TY  - CONF
AU  - Moros, Alejandro José Mahía
AU  - Engsted Kiib, Anders
AU  - Nišavić, Marija
AU  - Palmfeldt, Johan
AU  - Poulsen, Thomas
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12948
UR  - https://pure.au.dk/portal/en/publications/a-stable-%CE%B1-lactam-as-electrophilic-warhead-for-bioconjugation-and-2
AB  - Electrophilic warheads are one of the key pillars upon which chemical biology is founded, constituting the anchor point for the design of targeted covalent inhibitors, the identification of novel therapeutic targets, and the development of a wide diversity of bioconjugation and proteomic profiling techniques.[1] Within the panorama of continuous expansion of chemical biology applications, a great interest has grown in the discovery of new biologically relevant electrophilic warheads that contribute to broaden the current scope of action. That is the case of 3-membered N-heterocyclic compounds, whose electronic properties and structural strain trigger their potential as chemical tools in biological research.[2,3] However, up to date, there aren´t known utilities within this field for a potentially relevant member of the aforementioned family: the α-lactams. Here we show how an α-lactam reagent can be efficiently employed in the framework of bioconjugation and proteomic profiling. We have designed and synthesised a stable α-lactam (AM2) compatible with aqueous buffers and studied the reaction outcome and kinetics with benzylamine and benzyl mercaptane under different conditions. Higher reactivity was detected with the latter. We have further demonstrated that AM2 is attached to free cysteine residues in peptides, potentially as a thioester. Additionally, liver carboxylesterase 1 (CES1), with key roles in both endo- and xenobiotic metabolism,[4] was found as a selective target for AM2 in HepG2 cells and cell lysate. All in all, we anticipate AM2 to be a starting point for the development of new and more sophisticated α-lactam-based electrophilic probes for their use in covalent chemical biology.
C3  - 22nd Tetrahedron Symposium
T1  - A stable α-lactam as electrophilic warhead for bioconjugation and proteomic profiling
UR  - https://hdl.handle.net/21.15107/rcub_vinar_12948
ER  - 

@conference{
author = "Moros, Alejandro José Mahía and Engsted Kiib, Anders and Nišavić, Marija and Palmfeldt, Johan and Poulsen, Thomas",
year = "2022",
abstract = "Electrophilic warheads are one of the key pillars upon which chemical biology is founded, constituting the anchor point for the design of targeted covalent inhibitors, the identification of novel therapeutic targets, and the development of a wide diversity of bioconjugation and proteomic profiling techniques.[1] Within the panorama of continuous expansion of chemical biology applications, a great interest has grown in the discovery of new biologically relevant electrophilic warheads that contribute to broaden the current scope of action. That is the case of 3-membered N-heterocyclic compounds, whose electronic properties and structural strain trigger their potential as chemical tools in biological research.[2,3] However, up to date, there aren´t known utilities within this field for a potentially relevant member of the aforementioned family: the α-lactams. Here we show how an α-lactam reagent can be efficiently employed in the framework of bioconjugation and proteomic profiling. We have designed and synthesised a stable α-lactam (AM2) compatible with aqueous buffers and studied the reaction outcome and kinetics with benzylamine and benzyl mercaptane under different conditions. Higher reactivity was detected with the latter. We have further demonstrated that AM2 is attached to free cysteine residues in peptides, potentially as a thioester. Additionally, liver carboxylesterase 1 (CES1), with key roles in both endo- and xenobiotic metabolism,[4] was found as a selective target for AM2 in HepG2 cells and cell lysate. All in all, we anticipate AM2 to be a starting point for the development of new and more sophisticated α-lactam-based electrophilic probes for their use in covalent chemical biology.",
journal = "22nd Tetrahedron Symposium",
title = "A stable α-lactam as electrophilic warhead for bioconjugation and proteomic profiling",
url = "https://hdl.handle.net/21.15107/rcub_vinar_12948"
}

Moros, A. J. M., Engsted Kiib, A., Nišavić, M., Palmfeldt, J.,& Poulsen, T.. (2022). A stable α-lactam as electrophilic warhead for bioconjugation and proteomic profiling. in 22nd Tetrahedron Symposium.
https://hdl.handle.net/21.15107/rcub_vinar_12948

Moros AJM, Engsted Kiib A, Nišavić M, Palmfeldt J, Poulsen T. A stable α-lactam as electrophilic warhead for bioconjugation and proteomic profiling. in 22nd Tetrahedron Symposium. 2022;.
https://hdl.handle.net/21.15107/rcub_vinar_12948 .

Moros, Alejandro José Mahía, Engsted Kiib, Anders, Nišavić, Marija, Palmfeldt, Johan, Poulsen, Thomas, "A stable α-lactam as electrophilic warhead for bioconjugation and proteomic profiling" in 22nd Tetrahedron Symposium (2022),
https://hdl.handle.net/21.15107/rcub_vinar_12948 .

TY  - CONF
AU  - Moros, Alejandro José Mahía
AU  - Kiib, Anders Engsted
AU  - Nišavić, Marija
AU  - Palmfeldt, Johan
AU  - Poulsen, Thomas
PY  - 2022
UR  - https://pure.au.dk/portal/en/publications/studies-on-the-applicability-of-a-stable-alpha-lactam-as-electrop
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12949
C3  - The Danish Chemical Society Annual Meeting 2022
T1  - Studies on the applicability of a stable alpha-lactam as electrophilic probe for bioconjugation and proteomic profiling
UR  - https://hdl.handle.net/21.15107/rcub_vinar_12949
ER  - 

@conference{
author = "Moros, Alejandro José Mahía and Kiib, Anders Engsted and Nišavić, Marija and Palmfeldt, Johan and Poulsen, Thomas",
year = "2022",
journal = "The Danish Chemical Society Annual Meeting 2022",
title = "Studies on the applicability of a stable alpha-lactam as electrophilic probe for bioconjugation and proteomic profiling",
url = "https://hdl.handle.net/21.15107/rcub_vinar_12949"
}

Moros, A. J. M., Kiib, A. E., Nišavić, M., Palmfeldt, J.,& Poulsen, T.. (2022). Studies on the applicability of a stable alpha-lactam as electrophilic probe for bioconjugation and proteomic profiling. in The Danish Chemical Society Annual Meeting 2022.
https://hdl.handle.net/21.15107/rcub_vinar_12949

Moros AJM, Kiib AE, Nišavić M, Palmfeldt J, Poulsen T. Studies on the applicability of a stable alpha-lactam as electrophilic probe for bioconjugation and proteomic profiling. in The Danish Chemical Society Annual Meeting 2022. 2022;.
https://hdl.handle.net/21.15107/rcub_vinar_12949 .

Moros, Alejandro José Mahía, Kiib, Anders Engsted, Nišavić, Marija, Palmfeldt, Johan, Poulsen, Thomas, "Studies on the applicability of a stable alpha-lactam as electrophilic probe for bioconjugation and proteomic profiling" in The Danish Chemical Society Annual Meeting 2022 (2022),
https://hdl.handle.net/21.15107/rcub_vinar_12949 .

TY  - JOUR
AU  - Duvnjak, Marija
AU  - Butorac, Ana
AU  - Kljak, Kristina
AU  - Nišavić, Marija
AU  - Cindrić, Mario
AU  - Grbeša, Darko
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10483
AB  - The starch availability and nutritional value of corn (Zea mays L.) are affected by zein proteins. The aim of the study was to see whether the proposed reduction of γ-zeins during the fermentation of silages is a result of either the enzymatic proteolytic activity or of the acidic environment, and how this reduction affects starch availability and degradability in high-moisture corn. A mass spectrometry (MS) technique was used to quantify the 16- and 27-kDa γ-zeins. Briefly, two-dimensional gel electrophoresis (2-DE) was used for γ-zein separation, followed by densitometry for protein quantification and matrix-assisted laser desorption ionization time-of-flight MS (MALDI-TOF/TOF) for protein identification. The results show that the reduction in γ-zeins induced by the ensiling led to a more pronounced starch availability and in vitro degradation, and this reduction was dependent on the type of proteolysis. More specifically, the results indicate that the reduction of γ-zeins in the ensiled corn was primarily driven by the enzymatic proteolysis. Furthermore, we demonstrated that 2-DE followed by densitometric quantification and the mass spectrometry analysis for protein identification can be used as a state-of-the-art method for γ-zein evaluation both in fresh and fermented/ensiled corn samples.
T2  - Fermentation
T1  - The Evaluation of γ-Zein Reduction Using Mass Spectrometry—The Influence of Proteolysis Type in Relation to Starch Degradability in Silages
VL  - 8
IS  - 10
SP  - 551
DO  - 10.3390/fermentation8100551
ER  - 

@article{
author = "Duvnjak, Marija and Butorac, Ana and Kljak, Kristina and Nišavić, Marija and Cindrić, Mario and Grbeša, Darko",
year = "2022",
abstract = "The starch availability and nutritional value of corn (Zea mays L.) are affected by zein proteins. The aim of the study was to see whether the proposed reduction of γ-zeins during the fermentation of silages is a result of either the enzymatic proteolytic activity or of the acidic environment, and how this reduction affects starch availability and degradability in high-moisture corn. A mass spectrometry (MS) technique was used to quantify the 16- and 27-kDa γ-zeins. Briefly, two-dimensional gel electrophoresis (2-DE) was used for γ-zein separation, followed by densitometry for protein quantification and matrix-assisted laser desorption ionization time-of-flight MS (MALDI-TOF/TOF) for protein identification. The results show that the reduction in γ-zeins induced by the ensiling led to a more pronounced starch availability and in vitro degradation, and this reduction was dependent on the type of proteolysis. More specifically, the results indicate that the reduction of γ-zeins in the ensiled corn was primarily driven by the enzymatic proteolysis. Furthermore, we demonstrated that 2-DE followed by densitometric quantification and the mass spectrometry analysis for protein identification can be used as a state-of-the-art method for γ-zein evaluation both in fresh and fermented/ensiled corn samples.",
journal = "Fermentation",
title = "The Evaluation of γ-Zein Reduction Using Mass Spectrometry—The Influence of Proteolysis Type in Relation to Starch Degradability in Silages",
volume = "8",
number = "10",
pages = "551",
doi = "10.3390/fermentation8100551"
}

Duvnjak, M., Butorac, A., Kljak, K., Nišavić, M., Cindrić, M.,& Grbeša, D.. (2022). The Evaluation of γ-Zein Reduction Using Mass Spectrometry—The Influence of Proteolysis Type in Relation to Starch Degradability in Silages. in Fermentation, 8(10), 551.
https://doi.org/10.3390/fermentation8100551

Duvnjak M, Butorac A, Kljak K, Nišavić M, Cindrić M, Grbeša D. The Evaluation of γ-Zein Reduction Using Mass Spectrometry—The Influence of Proteolysis Type in Relation to Starch Degradability in Silages. in Fermentation. 2022;8(10):551.
doi:10.3390/fermentation8100551 .

Duvnjak, Marija, Butorac, Ana, Kljak, Kristina, Nišavić, Marija, Cindrić, Mario, Grbeša, Darko, "The Evaluation of γ-Zein Reduction Using Mass Spectrometry—The Influence of Proteolysis Type in Relation to Starch Degradability in Silages" in Fermentation, 8, no. 10 (2022):551,
https://doi.org/10.3390/fermentation8100551 . .

TY  - JOUR
AU  - Gulicovski, Jelena J.
AU  - Nenadović, Snežana S.
AU  - Kljajević, Ljiljana M.
AU  - Mirković, Miljana M.
AU  - Nišavić, Marija
AU  - Kragović, Milan M.
AU  - Stojmenović, Marija
PY  - 2020
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8480
AB  - As a material for application in the life sciences, a new composite material, geopolymer/CeO2 (GP_CeO2), was synthesized as a potential low-cost solid electrolyte for application in solid oxide fuel cells operating in intermediate temperature (IT-SOFC). The new materials were obtained from alkali-activated metakaolin (calcined clay) in the presence of CeO2 powders (x = 10%). Besides the commercial CeO2 powder, as a source of ceria, two differently synthesized CeO2 powders also were used: CeO2 synthesized by modified glycine nitrate procedure (MGNP) and self-propagating reaction at room temperature (SPRT). The structural, morphological, and electrical properties of pure and GP_CeO2-type samples were investigated by X-ray powder diffraction (XRPD), Fourier transform infrared (FTIR), BET, differential thermal and thermogravimetric analysis (DTA/TGA), scanning electron microscopy (FE-SEM), energy dispersive spectrometer (EDS), and method complex impedance (EIS). XRPD and matrix-assisted laser desorption and ionization time-of-flight (MALDI-TOF) analysis confirmed the formation of solid phase CeO2. The BET, DTA/TGA, FE-SEM, and EDS results indicated that particles of CeO2 were stabile interconnected and form a continuous conductive path, which was confirmed by the EIS method. The highest conductivity of 1.86 × 10−2 Ω−1 cm−1 was obtained for the sample GP_CeO2_MGNP at 700 °C. The corresponding value of activation energy for conductivity was 0.26 eV in the temperature range 500–700 °C.
T2  - Polymers
T1  - Geopolymer/CeO2 as Solid Electrolyte for IT-SOFC
VL  - 12
IS  - 1
SP  - 248
DO  - 10.3390/polym12010248
ER  - 

@article{
author = "Gulicovski, Jelena J. and Nenadović, Snežana S. and Kljajević, Ljiljana M. and Mirković, Miljana M. and Nišavić, Marija and Kragović, Milan M. and Stojmenović, Marija",
year = "2020",
abstract = "As a material for application in the life sciences, a new composite material, geopolymer/CeO2 (GP_CeO2), was synthesized as a potential low-cost solid electrolyte for application in solid oxide fuel cells operating in intermediate temperature (IT-SOFC). The new materials were obtained from alkali-activated metakaolin (calcined clay) in the presence of CeO2 powders (x = 10%). Besides the commercial CeO2 powder, as a source of ceria, two differently synthesized CeO2 powders also were used: CeO2 synthesized by modified glycine nitrate procedure (MGNP) and self-propagating reaction at room temperature (SPRT). The structural, morphological, and electrical properties of pure and GP_CeO2-type samples were investigated by X-ray powder diffraction (XRPD), Fourier transform infrared (FTIR), BET, differential thermal and thermogravimetric analysis (DTA/TGA), scanning electron microscopy (FE-SEM), energy dispersive spectrometer (EDS), and method complex impedance (EIS). XRPD and matrix-assisted laser desorption and ionization time-of-flight (MALDI-TOF) analysis confirmed the formation of solid phase CeO2. The BET, DTA/TGA, FE-SEM, and EDS results indicated that particles of CeO2 were stabile interconnected and form a continuous conductive path, which was confirmed by the EIS method. The highest conductivity of 1.86 × 10−2 Ω−1 cm−1 was obtained for the sample GP_CeO2_MGNP at 700 °C. The corresponding value of activation energy for conductivity was 0.26 eV in the temperature range 500–700 °C.",
journal = "Polymers",
title = "Geopolymer/CeO2 as Solid Electrolyte for IT-SOFC",
volume = "12",
number = "1",
pages = "248",
doi = "10.3390/polym12010248"
}

Gulicovski, J. J., Nenadović, S. S., Kljajević, L. M., Mirković, M. M., Nišavić, M., Kragović, M. M.,& Stojmenović, M.. (2020). Geopolymer/CeO2 as Solid Electrolyte for IT-SOFC. in Polymers, 12(1), 248.
https://doi.org/10.3390/polym12010248

Gulicovski JJ, Nenadović SS, Kljajević LM, Mirković MM, Nišavić M, Kragović MM, Stojmenović M. Geopolymer/CeO2 as Solid Electrolyte for IT-SOFC. in Polymers. 2020;12(1):248.
doi:10.3390/polym12010248 .

Gulicovski, Jelena J., Nenadović, Snežana S., Kljajević, Ljiljana M., Mirković, Miljana M., Nišavić, Marija, Kragović, Milan M., Stojmenović, Marija, "Geopolymer/CeO2 as Solid Electrolyte for IT-SOFC" in Polymers, 12, no. 1 (2020):248,
https://doi.org/10.3390/polym12010248 . .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10180
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/c7mt00330g
ER  - 

@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/c7mt00330g"
}

Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics, 10(4), 587-594.
https://doi.org/10.1039/c7mt00330g

Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics. 2018;10(4):587-594.
doi:10.1039/c7mt00330g .

Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" in Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/c7mt00330g . .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Stoiljković, Milovan
AU  - Crnolatac, Ivo
AU  - Milošević, Maja
AU  - Rilak, Ana
AU  - Masnikosa, Romana
PY  - 2018
UR  - http://linkinghub.elsevier.com/retrieve/pii/S1878535216301198
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7665
AB  - Three coordination compounds of ruthenium(II), belonging to a recently synthesised series of water-soluble compounds of general formula mer-{[}Ru(L3)(N-N) Cl] Cl, where L3 = 4'-chloro2,2': 6', 200-terpyridine (Cl-tpy), N-N= ethylenediamine (en), 1,2-diaminocyclohexane (dach) or 2,2'bipyridine (bpy), have shown strong binding to calf thymus DNA and moderate in vitro cytotoxicity towards cancer cell lines. Knowing that serum proteins play a crucial role in the transport and deactivation of ruthenium drugs, we have conducted a detailed study of their interactions with two major metal-transporting serum proteins, albumin and transferrin, and it is presented herein. Ruthenated protein adducts were formed with various concentrations of the three compounds and then separated from the unbound portions by ultrafiltration through 10 kDa cut-off centrifugal filter units. The stoichiometry of binding was determined using inductively coupled plasma optical emission spectrometry. One mol of albumin bound up to 7, 8.5 and 1.5 mol of compound 1 ({[}Ru(Cltpy)(en) Cl]{[}Cl]), 2 ({[}Ru(Cl-tpy)(dach) Cl]{[}Cl] and 3 ({[}Ru(Cl-tpy)(bpy) Cl]{[}Cl]), respectively. One mol of transferrin bound up to 3, 3.5 and 0.4 mol of 1, 2 and 3, respectively. The affinity of albumin and transferrin for the three ruthenium compounds was evaluated using fluorescence quenching. The binding constants for 1 and 2 lay within the range 10(4) -10(5) M - 1, suggesting moderate-to-strong attachment to albumin. Both compounds showed much lower affinity for transferrin (10(2) -10(3) M - 1). Compound 3 bound weakly to each studied protein. High resolution ESI qTOF mass spectra of albumin before and after binding of 1 revealed the high stoichiometry of binding. Although the binding of the compounds 1-3 to albumin and transferrin did not affect proteins' secondary structure much, their tertiary structures underwent some alterations, as deduced from the circular dichroism study. Changes in the stability of albumin, after binding to compounds 1-3 were examined by differential scanning calorimetry. (C) 2016 The Authors. Production and hosting by Elsevier B. V. on behalf of King Saud University. This is an open access article under theCCBY-NC-NDlicense.
T2  - Arabian Journal of Chemistry
T1  - Highly water-soluble ruthenium(II) terpyridine coordination compounds form stable adducts with blood-borne metal transporting proteins
VL  - 11
IS  - 3
SP  - 291
EP  - 304
DO  - 10.1016/j.arabjc.2016.07.021
ER  - 

@article{
author = "Nišavić, Marija and Stoiljković, Milovan and Crnolatac, Ivo and Milošević, Maja and Rilak, Ana and Masnikosa, Romana",
year = "2018",
abstract = "Three coordination compounds of ruthenium(II), belonging to a recently synthesised series of water-soluble compounds of general formula mer-{[}Ru(L3)(N-N) Cl] Cl, where L3 = 4'-chloro2,2': 6', 200-terpyridine (Cl-tpy), N-N= ethylenediamine (en), 1,2-diaminocyclohexane (dach) or 2,2'bipyridine (bpy), have shown strong binding to calf thymus DNA and moderate in vitro cytotoxicity towards cancer cell lines. Knowing that serum proteins play a crucial role in the transport and deactivation of ruthenium drugs, we have conducted a detailed study of their interactions with two major metal-transporting serum proteins, albumin and transferrin, and it is presented herein. Ruthenated protein adducts were formed with various concentrations of the three compounds and then separated from the unbound portions by ultrafiltration through 10 kDa cut-off centrifugal filter units. The stoichiometry of binding was determined using inductively coupled plasma optical emission spectrometry. One mol of albumin bound up to 7, 8.5 and 1.5 mol of compound 1 ({[}Ru(Cltpy)(en) Cl]{[}Cl]), 2 ({[}Ru(Cl-tpy)(dach) Cl]{[}Cl] and 3 ({[}Ru(Cl-tpy)(bpy) Cl]{[}Cl]), respectively. One mol of transferrin bound up to 3, 3.5 and 0.4 mol of 1, 2 and 3, respectively. The affinity of albumin and transferrin for the three ruthenium compounds was evaluated using fluorescence quenching. The binding constants for 1 and 2 lay within the range 10(4) -10(5) M - 1, suggesting moderate-to-strong attachment to albumin. Both compounds showed much lower affinity for transferrin (10(2) -10(3) M - 1). Compound 3 bound weakly to each studied protein. High resolution ESI qTOF mass spectra of albumin before and after binding of 1 revealed the high stoichiometry of binding. Although the binding of the compounds 1-3 to albumin and transferrin did not affect proteins' secondary structure much, their tertiary structures underwent some alterations, as deduced from the circular dichroism study. Changes in the stability of albumin, after binding to compounds 1-3 were examined by differential scanning calorimetry. (C) 2016 The Authors. Production and hosting by Elsevier B. V. on behalf of King Saud University. This is an open access article under theCCBY-NC-NDlicense.",
journal = "Arabian Journal of Chemistry",
title = "Highly water-soluble ruthenium(II) terpyridine coordination compounds form stable adducts with blood-borne metal transporting proteins",
volume = "11",
number = "3",
pages = "291-304",
doi = "10.1016/j.arabjc.2016.07.021"
}

Nišavić, M., Stoiljković, M., Crnolatac, I., Milošević, M., Rilak, A.,& Masnikosa, R.. (2018). Highly water-soluble ruthenium(II) terpyridine coordination compounds form stable adducts with blood-borne metal transporting proteins. in Arabian Journal of Chemistry, 11(3), 291-304.
https://doi.org/10.1016/j.arabjc.2016.07.021

Nišavić M, Stoiljković M, Crnolatac I, Milošević M, Rilak A, Masnikosa R. Highly water-soluble ruthenium(II) terpyridine coordination compounds form stable adducts with blood-borne metal transporting proteins. in Arabian Journal of Chemistry. 2018;11(3):291-304.
doi:10.1016/j.arabjc.2016.07.021 .

Nišavić, Marija, Stoiljković, Milovan, Crnolatac, Ivo, Milošević, Maja, Rilak, Ana, Masnikosa, Romana, "Highly water-soluble ruthenium(II) terpyridine coordination compounds form stable adducts with blood-borne metal transporting proteins" in Arabian Journal of Chemistry, 11, no. 3 (2018):291-304,
https://doi.org/10.1016/j.arabjc.2016.07.021 . .

TY  - JOUR
AU  - Rajčić, Boris
AU  - Dimitrijević, Silvana B.
AU  - Petković, Marijana
AU  - Nišavić, Marija
AU  - Cindrić, Mario
AU  - Veljković, Filip M.
AU  - Veličković, Suzana
PY  - 2018
UR  - http://link.springer.com/10.1007/s11082-018-1476-2
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7687
AB  - In this work, a simple way for study the possibility of formation a vapor cluster species of tetrachloroauric acid (HAuCl4), using the laser ablation in the absence of a buffer or reactive atmosphere, and without a postablation supersonic expansion on a commercial matrix assisted laser desorption/ionization time-of-flight mass spectrometer, is reported. Tetrachloroauric acid is known as precursor for the synthesis of gold nanostructures and the complex salts; therefore it is an important task to discover and quantify the species arising from HAuCl4, in order to understand their role in the gold assisted reactions. Mass spectrum of HAuCl4in a reflector negative-ion mode contains the hydrated mono- and dinuclear gold clusters in the m/z range 286–436, and gold chloride clusters in the m/z range 447–795. In the first part of spectrum, m/z range 286–436, the hydrated gold cluster species of type Aun−(H2O)m(n = 1–2; m = 1, 2, 5, 7, 8) and [Aun(OH)k]−(H2O)m(n = 1–2; k = 1–2; m = 1, 4–8) were found. Besides that, there are gold chloride clusters with general formula [AuHr(HCl)2]−(H2O)m(m = 1–5; 8–9; r = 0–2) in this part of spectrum. In the second part of spectrum, the m/z range 447–795, only gold chloride clusters were obtained. Their general formulae can be written as [AuClt(HCl)v]−(H2O)m(t = 1–4; v = 5–8; m = 2–4, 6–8) and [Aun(HCl)v]−(H2O)m(n = 1–2, v = 4–5, m = 1–2, 5, 7). The analysis of concentration effects on the LDI mass spectra of gold clusters reveals that the relative intensities of signals for the mono- and dinuclear Au clusters increase with decreasing the concentration of water HAuCl4solutions.
T2  - Optical and Quantum Electronics
T1  - Gold chloride cluster ions generated by vacuum laser ablation
VL  - 50
IS  - 5
SP  - 218
DO  - 10.1007/s11082-018-1476-2
ER  - 

@article{
author = "Rajčić, Boris and Dimitrijević, Silvana B. and Petković, Marijana and Nišavić, Marija and Cindrić, Mario and Veljković, Filip M. and Veličković, Suzana",
year = "2018",
abstract = "In this work, a simple way for study the possibility of formation a vapor cluster species of tetrachloroauric acid (HAuCl4), using the laser ablation in the absence of a buffer or reactive atmosphere, and without a postablation supersonic expansion on a commercial matrix assisted laser desorption/ionization time-of-flight mass spectrometer, is reported. Tetrachloroauric acid is known as precursor for the synthesis of gold nanostructures and the complex salts; therefore it is an important task to discover and quantify the species arising from HAuCl4, in order to understand their role in the gold assisted reactions. Mass spectrum of HAuCl4in a reflector negative-ion mode contains the hydrated mono- and dinuclear gold clusters in the m/z range 286–436, and gold chloride clusters in the m/z range 447–795. In the first part of spectrum, m/z range 286–436, the hydrated gold cluster species of type Aun−(H2O)m(n = 1–2; m = 1, 2, 5, 7, 8) and [Aun(OH)k]−(H2O)m(n = 1–2; k = 1–2; m = 1, 4–8) were found. Besides that, there are gold chloride clusters with general formula [AuHr(HCl)2]−(H2O)m(m = 1–5; 8–9; r = 0–2) in this part of spectrum. In the second part of spectrum, the m/z range 447–795, only gold chloride clusters were obtained. Their general formulae can be written as [AuClt(HCl)v]−(H2O)m(t = 1–4; v = 5–8; m = 2–4, 6–8) and [Aun(HCl)v]−(H2O)m(n = 1–2, v = 4–5, m = 1–2, 5, 7). The analysis of concentration effects on the LDI mass spectra of gold clusters reveals that the relative intensities of signals for the mono- and dinuclear Au clusters increase with decreasing the concentration of water HAuCl4solutions.",
journal = "Optical and Quantum Electronics",
title = "Gold chloride cluster ions generated by vacuum laser ablation",
volume = "50",
number = "5",
pages = "218",
doi = "10.1007/s11082-018-1476-2"
}

Rajčić, B., Dimitrijević, S. B., Petković, M., Nišavić, M., Cindrić, M., Veljković, F. M.,& Veličković, S.. (2018). Gold chloride cluster ions generated by vacuum laser ablation. in Optical and Quantum Electronics, 50(5), 218.
https://doi.org/10.1007/s11082-018-1476-2

Rajčić B, Dimitrijević SB, Petković M, Nišavić M, Cindrić M, Veljković FM, Veličković S. Gold chloride cluster ions generated by vacuum laser ablation. in Optical and Quantum Electronics. 2018;50(5):218.
doi:10.1007/s11082-018-1476-2 .

Rajčić, Boris, Dimitrijević, Silvana B., Petković, Marijana, Nišavić, Marija, Cindrić, Mario, Veljković, Filip M., Veličković, Suzana, "Gold chloride cluster ions generated by vacuum laser ablation" in Optical and Quantum Electronics, 50, no. 5 (2018):218,
https://doi.org/10.1007/s11082-018-1476-2 . .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - http://xlink.rsc.org/?DOI=C7MT00330G
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7615
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/C7MT00330G
ER  - 

@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/C7MT00330G"
}

Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics, 10(4), 587-594.
https://doi.org/10.1039/C7MT00330G

Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics. 2018;10(4):587-594.
doi:10.1039/C7MT00330G .

Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" in Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/C7MT00330G . .

TY  - CONF
AU  - Matijević, Milica
AU  - Cindrić, Marina
AU  - Petković, Marijana
AU  - Nišavić, Marija
PY  - 2018
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7921
C3  - FEBS OPEN BIO
T1  - Structural characterization of transferrin-bound ruthenium(II) terpyridine complexes
VL  - 8
IS  - 1
SP  - 406+
DO  - 10.1002/2211-5463.12453
ER  - 

@conference{
author = "Matijević, Milica and Cindrić, Marina and Petković, Marijana and Nišavić, Marija",
year = "2018",
journal = "FEBS OPEN BIO",
title = "Structural characterization of transferrin-bound ruthenium(II) terpyridine complexes",
volume = "8",
number = "1",
pages = "406+",
doi = "10.1002/2211-5463.12453"
}

Matijević, M., Cindrić, M., Petković, M.,& Nišavić, M.. (2018). Structural characterization of transferrin-bound ruthenium(II) terpyridine complexes. in FEBS OPEN BIO, 8(1), 406+.
https://doi.org/10.1002/2211-5463.12453

Matijević M, Cindrić M, Petković M, Nišavić M. Structural characterization of transferrin-bound ruthenium(II) terpyridine complexes. in FEBS OPEN BIO. 2018;8(1):406+.
doi:10.1002/2211-5463.12453 .

Matijević, Milica, Cindrić, Marina, Petković, Marijana, Nišavić, Marija, "Structural characterization of transferrin-bound ruthenium(II) terpyridine complexes" in FEBS OPEN BIO, 8, no. 1 (2018):406+,
https://doi.org/10.1002/2211-5463.12453 . .

TY  - JOUR
AU  - Dimkić, Ivica
AU  - Stanković, Slavka
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Ristivojević, Petar
AU  - Fira, Đorđe
AU  - Berić, Tanja
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1665
T2  - Frontiers in Microbiology
T1  - Corrigendum: The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)
VL  - 8
DO  - 10.3389/fmicb.2017.01500
ER  - 

@article{
author = "Dimkić, Ivica and Stanković, Slavka and Nišavić, Marija and Petković, Marijana and Ristivojević, Petar and Fira, Đorđe and Berić, Tanja",
year = "2017",
journal = "Frontiers in Microbiology",
title = "Corrigendum: The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)",
volume = "8",
doi = "10.3389/fmicb.2017.01500"
}

Dimkić, I., Stanković, S., Nišavić, M., Petković, M., Ristivojević, P., Fira, Đ.,& Berić, T.. (2017). Corrigendum: The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017). in Frontiers in Microbiology, 8.
https://doi.org/10.3389/fmicb.2017.01500

Dimkić I, Stanković S, Nišavić M, Petković M, Ristivojević P, Fira Đ, Berić T. Corrigendum: The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017). in Frontiers in Microbiology. 2017;8.
doi:10.3389/fmicb.2017.01500 .

Dimkić, Ivica, Stanković, Slavka, Nišavić, Marija, Petković, Marijana, Ristivojević, Petar, Fira, Đorđe, Berić, Tanja, "Corrigendum: The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)" in Frontiers in Microbiology, 8 (2017),
https://doi.org/10.3389/fmicb.2017.01500 . .

TY  - JOUR
AU  - Rakić-Kostić, Tijana M.
AU  - Bogojeski, Jovana V.
AU  - Popović, Iva A.
AU  - Nešić, Maja D.
AU  - Rajčić, Boris
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Veličković, Suzana
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1362
AB  - This paper presents optimization of matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometer (MS) instrumental parameters for the analysis of chloro(2,2 , 2 -terpyridine) palladium(II) chloride dihydrate complex applying design of experiments methodology (DoE). This complex is of interest for potential use in the cancer therapy. DoE methodology was proved to succeed in optimization of many complex analytical problems. However, it has been poorly used for MALDI-TOF-MS optimization up to now. The theoretical mathematical relationships which explain the influence of important experimental factors (laser energy, grid voltage and number of laser shots) on the selected responses (signal to noise - S/N ratio and the resolution - R of the leading peak) is established. The optimal instrumental settings providing maximal S/N and R are identified and experimentally verified.
T2  - Hemijska industrija
T1  - Experimental design for optimizing MALDI-TOF-MS analysis of palladium complexes
VL  - 71
IS  - 4
SP  - 281
EP  - 288
DO  - 10.2298/HEMIND160614038R
ER  - 

@article{
author = "Rakić-Kostić, Tijana M. and Bogojeski, Jovana V. and Popović, Iva A. and Nešić, Maja D. and Rajčić, Boris and Nišavić, Marija and Petković, Marijana and Veličković, Suzana",
year = "2017",
abstract = "This paper presents optimization of matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometer (MS) instrumental parameters for the analysis of chloro(2,2 , 2 -terpyridine) palladium(II) chloride dihydrate complex applying design of experiments methodology (DoE). This complex is of interest for potential use in the cancer therapy. DoE methodology was proved to succeed in optimization of many complex analytical problems. However, it has been poorly used for MALDI-TOF-MS optimization up to now. The theoretical mathematical relationships which explain the influence of important experimental factors (laser energy, grid voltage and number of laser shots) on the selected responses (signal to noise - S/N ratio and the resolution - R of the leading peak) is established. The optimal instrumental settings providing maximal S/N and R are identified and experimentally verified.",
journal = "Hemijska industrija",
title = "Experimental design for optimizing MALDI-TOF-MS analysis of palladium complexes",
volume = "71",
number = "4",
pages = "281-288",
doi = "10.2298/HEMIND160614038R"
}

Rakić-Kostić, T. M., Bogojeski, J. V., Popović, I. A., Nešić, M. D., Rajčić, B., Nišavić, M., Petković, M.,& Veličković, S.. (2017). Experimental design for optimizing MALDI-TOF-MS analysis of palladium complexes. in Hemijska industrija, 71(4), 281-288.
https://doi.org/10.2298/HEMIND160614038R

Rakić-Kostić TM, Bogojeski JV, Popović IA, Nešić MD, Rajčić B, Nišavić M, Petković M, Veličković S. Experimental design for optimizing MALDI-TOF-MS analysis of palladium complexes. in Hemijska industrija. 2017;71(4):281-288.
doi:10.2298/HEMIND160614038R .

Rakić-Kostić, Tijana M., Bogojeski, Jovana V., Popović, Iva A., Nešić, Maja D., Rajčić, Boris, Nišavić, Marija, Petković, Marijana, Veličković, Suzana, "Experimental design for optimizing MALDI-TOF-MS analysis of palladium complexes" in Hemijska industrija, 71, no. 4 (2017):281-288,
https://doi.org/10.2298/HEMIND160614038R . .

TY  - JOUR
AU  - Dimkić, Ivica
AU  - Stanković, Slavka
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Ristivojević, Petar
AU  - Fira, Đorđe
AU  - Berić, Tanja
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1591
AB  - In this study the efficacy of two different methods for extracting lipopeptides produced by five Bacillus strains-ethyl acetate extraction, and acid precipitation followed by methanol extraction-was investigated using mass spectrometry. High performance thin layer chromatography (HPTLC) was also used for the simultaneous separation of complex mixtures of lipopeptide extracts and for the determination of antimicrobial activity of their components. The mass spectra clearly showed well-resolved groups of peaks corresponding to different lipopeptide families (kurstakins, iturins, surfactins, and fengycins). The ethyl acetate extracts produced the most favorable results. The extracts of SS-12.6, SS-13.1, and SS-38.4 showed the highest inhibition zones. An iturin analog is responsible for the inhibition of Xanthomonas arboricola and Pseudomonas syringae phytopathogenic strains. HPTLC bioautography effectively identified the active compounds from a mixture of lipopeptide extracts, proving in situ its potential for use in direct detection and determination of antimicrobials. In the test of potential synergism among individual extracts used in different mixtures, stronger antimicrobial effects were not observed. Biochemical and phylogenetic analysis clustered isolates SS-12.6, SS-13.1, SS-27.2, and SS-38.4 together with Bacillus amyloliquefaciens, while SS-10.7 was more closely related to Bacillus pumilus.
T2  - Frontiers in Microbiology
T1  - The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains
VL  - 8
DO  - 10.3389/fmicb.2017.00925
ER  - 

@article{
author = "Dimkić, Ivica and Stanković, Slavka and Nišavić, Marija and Petković, Marijana and Ristivojević, Petar and Fira, Đorđe and Berić, Tanja",
year = "2017",
abstract = "In this study the efficacy of two different methods for extracting lipopeptides produced by five Bacillus strains-ethyl acetate extraction, and acid precipitation followed by methanol extraction-was investigated using mass spectrometry. High performance thin layer chromatography (HPTLC) was also used for the simultaneous separation of complex mixtures of lipopeptide extracts and for the determination of antimicrobial activity of their components. The mass spectra clearly showed well-resolved groups of peaks corresponding to different lipopeptide families (kurstakins, iturins, surfactins, and fengycins). The ethyl acetate extracts produced the most favorable results. The extracts of SS-12.6, SS-13.1, and SS-38.4 showed the highest inhibition zones. An iturin analog is responsible for the inhibition of Xanthomonas arboricola and Pseudomonas syringae phytopathogenic strains. HPTLC bioautography effectively identified the active compounds from a mixture of lipopeptide extracts, proving in situ its potential for use in direct detection and determination of antimicrobials. In the test of potential synergism among individual extracts used in different mixtures, stronger antimicrobial effects were not observed. Biochemical and phylogenetic analysis clustered isolates SS-12.6, SS-13.1, SS-27.2, and SS-38.4 together with Bacillus amyloliquefaciens, while SS-10.7 was more closely related to Bacillus pumilus.",
journal = "Frontiers in Microbiology",
title = "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains",
volume = "8",
doi = "10.3389/fmicb.2017.00925"
}

Dimkić, I., Stanković, S., Nišavić, M., Petković, M., Ristivojević, P., Fira, Đ.,& Berić, T.. (2017). The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. in Frontiers in Microbiology, 8.
https://doi.org/10.3389/fmicb.2017.00925

Dimkić I, Stanković S, Nišavić M, Petković M, Ristivojević P, Fira Đ, Berić T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. in Frontiers in Microbiology. 2017;8.
doi:10.3389/fmicb.2017.00925 .

Dimkić, Ivica, Stanković, Slavka, Nišavić, Marija, Petković, Marijana, Ristivojević, Petar, Fira, Đorđe, Berić, Tanja, "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains" in Frontiers in Microbiology, 8 (2017),
https://doi.org/10.3389/fmicb.2017.00925 . .

TY  - JOUR
AU  - Ćoćić, Dušan
AU  - Jovanović, Snežana
AU  - Nišavić, Marija
AU  - Baskic, Dejan
AU  - Todorović, Danijela V.
AU  - Popovic, Suzana
AU  - Bugarčić, Živadin D.
AU  - Petrović, Biljana
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1758
AB  - Six new dinuclear Pd(II) complexes, [{Pd(2,2-bipy)Cl}(2)(mu-pz)](ClO4)2 (Pd1), [{Pd(dach)Cl}(2)(mu-pz)](ClO4)(2) (Pd2), [{Pd(en)Cl}(2)(mu-pz)] (ClO4)(2) (Pd3), [{Pd(2,2-bipy)Cl}(2)(mu-4,4-bipy)](ClO4)(2) (Pd4), [{Pd(dach)Cl}(2)(mu-4,4-bipy)] (ClO4)(2) (Pd5) and [{Pd(en)Cl-2(mu-4,4-bipy)](ClO4)(2) (Pd6) (where 2,2-bipy = 2,2-bipyridyl, pz = pyrazine, dach = trans-(+/-)-1,2-diaminocyclohexane, en = ethylenediamine, 4,4-bipy = 4,4-bipyridyl) have been synthesized and characterized by elemental microanalysis, IR, H-1 NMR and MALDI-TOF mass spectrometry. The pK(a) values of corresponding diaqua complexes were determined by spectrophotometric pH titration. Substitution reactions with thiourea (Tu), L-methionine (L-Met), L-cysteine (L-Cys), L-histidine (L-His) and guanosine-5-monophosphate (5-GMP) were studied under the pseudo-first order conditions at pH 7.2. Reactions of Pdl with Tu, L-Met and L-Cys were followed by decomposition of complexes, while structures of dinuclear complexes were preserved during the substitution with nitrogen donors. Interactions with calf-thymus DNA (CT DNA) were followed by absorption spectroscopy and fluorescence quenching measurements. All complexes can bind to CT-DNA exhibiting high intrinsic binding constants (K-b = 10(4)-10(5) M-1). Competitive studies with ethidium bromide (EB) have shown that complexes can displace DNA-bound EB. High values of binding constants towards bovine serum albumin protein (BSA) indicate good binding affinity. Finally, all complexes showed moderate to high cytotoxic activity against HeLa (human cervical epithelial carcinoma cell lines) and MDA-MB-231 (human breast epithelial carcinoma cell lines) tumor cell lines inducing apoptotic type cell death, whereas normal fibroblasts were significantly less sensitive. The impact on cell cycle of these cells was distinctive, where Pd4, Pd5 and Pd6 showed the most prominent effect arresting MDA-MB-231 (human lung fibroblast cell lines) cell in G1/S phase of cell cycle.
T2  - Journal of Inorganic Biochemistry
T1  - New dinuclear palladium(II) complexes: Studies of the nucleophilic substitution reactions, DNA/BSA interactions and cytotoxic activity
VL  - 175
SP  - 67
EP  - 79
DO  - 10.1016/j.jinorgbio.2017.07.009
ER  - 

@article{
author = "Ćoćić, Dušan and Jovanović, Snežana and Nišavić, Marija and Baskic, Dejan and Todorović, Danijela V. and Popovic, Suzana and Bugarčić, Živadin D. and Petrović, Biljana",
year = "2017",
abstract = "Six new dinuclear Pd(II) complexes, [{Pd(2,2-bipy)Cl}(2)(mu-pz)](ClO4)2 (Pd1), [{Pd(dach)Cl}(2)(mu-pz)](ClO4)(2) (Pd2), [{Pd(en)Cl}(2)(mu-pz)] (ClO4)(2) (Pd3), [{Pd(2,2-bipy)Cl}(2)(mu-4,4-bipy)](ClO4)(2) (Pd4), [{Pd(dach)Cl}(2)(mu-4,4-bipy)] (ClO4)(2) (Pd5) and [{Pd(en)Cl-2(mu-4,4-bipy)](ClO4)(2) (Pd6) (where 2,2-bipy = 2,2-bipyridyl, pz = pyrazine, dach = trans-(+/-)-1,2-diaminocyclohexane, en = ethylenediamine, 4,4-bipy = 4,4-bipyridyl) have been synthesized and characterized by elemental microanalysis, IR, H-1 NMR and MALDI-TOF mass spectrometry. The pK(a) values of corresponding diaqua complexes were determined by spectrophotometric pH titration. Substitution reactions with thiourea (Tu), L-methionine (L-Met), L-cysteine (L-Cys), L-histidine (L-His) and guanosine-5-monophosphate (5-GMP) were studied under the pseudo-first order conditions at pH 7.2. Reactions of Pdl with Tu, L-Met and L-Cys were followed by decomposition of complexes, while structures of dinuclear complexes were preserved during the substitution with nitrogen donors. Interactions with calf-thymus DNA (CT DNA) were followed by absorption spectroscopy and fluorescence quenching measurements. All complexes can bind to CT-DNA exhibiting high intrinsic binding constants (K-b = 10(4)-10(5) M-1). Competitive studies with ethidium bromide (EB) have shown that complexes can displace DNA-bound EB. High values of binding constants towards bovine serum albumin protein (BSA) indicate good binding affinity. Finally, all complexes showed moderate to high cytotoxic activity against HeLa (human cervical epithelial carcinoma cell lines) and MDA-MB-231 (human breast epithelial carcinoma cell lines) tumor cell lines inducing apoptotic type cell death, whereas normal fibroblasts were significantly less sensitive. The impact on cell cycle of these cells was distinctive, where Pd4, Pd5 and Pd6 showed the most prominent effect arresting MDA-MB-231 (human lung fibroblast cell lines) cell in G1/S phase of cell cycle.",
journal = "Journal of Inorganic Biochemistry",
title = "New dinuclear palladium(II) complexes: Studies of the nucleophilic substitution reactions, DNA/BSA interactions and cytotoxic activity",
volume = "175",
pages = "67-79",
doi = "10.1016/j.jinorgbio.2017.07.009"
}

Ćoćić, D., Jovanović, S., Nišavić, M., Baskic, D., Todorović, D. V., Popovic, S., Bugarčić, Ž. D.,& Petrović, B.. (2017). New dinuclear palladium(II) complexes: Studies of the nucleophilic substitution reactions, DNA/BSA interactions and cytotoxic activity. in Journal of Inorganic Biochemistry, 175, 67-79.
https://doi.org/10.1016/j.jinorgbio.2017.07.009

Ćoćić D, Jovanović S, Nišavić M, Baskic D, Todorović DV, Popovic S, Bugarčić ŽD, Petrović B. New dinuclear palladium(II) complexes: Studies of the nucleophilic substitution reactions, DNA/BSA interactions and cytotoxic activity. in Journal of Inorganic Biochemistry. 2017;175:67-79.
doi:10.1016/j.jinorgbio.2017.07.009 .

Ćoćić, Dušan, Jovanović, Snežana, Nišavić, Marija, Baskic, Dejan, Todorović, Danijela V., Popovic, Suzana, Bugarčić, Živadin D., Petrović, Biljana, "New dinuclear palladium(II) complexes: Studies of the nucleophilic substitution reactions, DNA/BSA interactions and cytotoxic activity" in Journal of Inorganic Biochemistry, 175 (2017):67-79,
https://doi.org/10.1016/j.jinorgbio.2017.07.009 . .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Hozić, Amela
AU  - Hameršak, Zdenko
AU  - Radić, Martina
AU  - Butorac, Ana
AU  - Duvnjak, Marija
AU  - Cindrić, Mario
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1552
AB  - Liquid chromatography coupled with electrospray ionization mass spectrometry (ESI-MS) is routinely used in proteomics research. Mass spectrometry-based peptide analysis is performed de facto in positive-ion mode, except for the analysis of some post-translationally modified peptides (e.g., phosphorylation and glycosylation). Collected mass spectrometry data after peptide negative ionization analysis is scarce, because of a lack of negatively charged amino acid side-chain residues that would enable efficient ionization (i.e., on average, every 10th amino acid residue is negatively charged). Also, several phenomena linked to negative ionization, such as corona discharge, arcing, and electrospray destabilization, because of the presence of polar mobile-phase solutions or acidic mobile-phase additives (e.g., formic or trifluoroacetic acid), reduce its use. Named phenomena influence microflow and nanoflow electrospray ionization (ESI) of peptides in a way that prevents the formation of negatively charged peptide ions. In this work, we have investigated the effects of post-column addition of isopropanol solutions of formaldehyde, 2,2-dimethylpropanal, ethyl methanoate, and 2-phenyl-2-oxoethanal as the negative-ion-mode mobile-phase modifiers for the analysis of peptides. According to the obtained data, all four modifiers exhibited significant enhancement of peptide negative ionization, while ethyl methanoate showed the best results. The proposed mechanism of action of the modifiers includes proton transfer reactions through oxonium ion formation. In this way, mobile phase protons are prevented from interfering with the process of negative ionization. To the best of our knowledge, this is the first study that describes the use and reaction mechanism of aforementioned modifiers for enhancement of peptide negative ionization.
T2  - Analytical Chemistry
T1  - High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions
VL  - 89
IS  - 9
SP  - 4847
EP  - 4854
DO  - 10.1021/acs.analchem.6b04466
ER  - 

@article{
author = "Nišavić, Marija and Hozić, Amela and Hameršak, Zdenko and Radić, Martina and Butorac, Ana and Duvnjak, Marija and Cindrić, Mario",
year = "2017",
abstract = "Liquid chromatography coupled with electrospray ionization mass spectrometry (ESI-MS) is routinely used in proteomics research. Mass spectrometry-based peptide analysis is performed de facto in positive-ion mode, except for the analysis of some post-translationally modified peptides (e.g., phosphorylation and glycosylation). Collected mass spectrometry data after peptide negative ionization analysis is scarce, because of a lack of negatively charged amino acid side-chain residues that would enable efficient ionization (i.e., on average, every 10th amino acid residue is negatively charged). Also, several phenomena linked to negative ionization, such as corona discharge, arcing, and electrospray destabilization, because of the presence of polar mobile-phase solutions or acidic mobile-phase additives (e.g., formic or trifluoroacetic acid), reduce its use. Named phenomena influence microflow and nanoflow electrospray ionization (ESI) of peptides in a way that prevents the formation of negatively charged peptide ions. In this work, we have investigated the effects of post-column addition of isopropanol solutions of formaldehyde, 2,2-dimethylpropanal, ethyl methanoate, and 2-phenyl-2-oxoethanal as the negative-ion-mode mobile-phase modifiers for the analysis of peptides. According to the obtained data, all four modifiers exhibited significant enhancement of peptide negative ionization, while ethyl methanoate showed the best results. The proposed mechanism of action of the modifiers includes proton transfer reactions through oxonium ion formation. In this way, mobile phase protons are prevented from interfering with the process of negative ionization. To the best of our knowledge, this is the first study that describes the use and reaction mechanism of aforementioned modifiers for enhancement of peptide negative ionization.",
journal = "Analytical Chemistry",
title = "High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions",
volume = "89",
number = "9",
pages = "4847-4854",
doi = "10.1021/acs.analchem.6b04466"
}

Nišavić, M., Hozić, A., Hameršak, Z., Radić, M., Butorac, A., Duvnjak, M.,& Cindrić, M.. (2017). High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions. in Analytical Chemistry, 89(9), 4847-4854.
https://doi.org/10.1021/acs.analchem.6b04466

Nišavić M, Hozić A, Hameršak Z, Radić M, Butorac A, Duvnjak M, Cindrić M. High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions. in Analytical Chemistry. 2017;89(9):4847-4854.
doi:10.1021/acs.analchem.6b04466 .

Nišavić, Marija, Hozić, Amela, Hameršak, Zdenko, Radić, Martina, Butorac, Ana, Duvnjak, Marija, Cindrić, Mario, "High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions" in Analytical Chemistry, 89, no. 9 (2017):4847-4854,
https://doi.org/10.1021/acs.analchem.6b04466 . .

TY  - CONF
AU  - Popović, Iva A.
AU  - Nešić, Mioljub V.
AU  - Nišavić, Marija
AU  - Petković, Marijana
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7113
C3  - FEBS Journal
T1  - Testing the best matrix/analyte combination for MALDI TOF mass spectrometric detection of steroid hormones, amino acids, vitamins and carbohydrates
VL  - 283
SP  - 166
EP  - 166
UR  - https://hdl.handle.net/21.15107/rcub_vinar_7113
ER  - 

@conference{
author = "Popović, Iva A. and Nešić, Mioljub V. and Nišavić, Marija and Petković, Marijana",
year = "2016",
journal = "FEBS Journal",
title = "Testing the best matrix/analyte combination for MALDI TOF mass spectrometric detection of steroid hormones, amino acids, vitamins and carbohydrates",
volume = "283",
pages = "166-166",
url = "https://hdl.handle.net/21.15107/rcub_vinar_7113"
}

Popović, I. A., Nešić, M. V., Nišavić, M.,& Petković, M.. (2016). Testing the best matrix/analyte combination for MALDI TOF mass spectrometric detection of steroid hormones, amino acids, vitamins and carbohydrates. in FEBS Journal, 283, 166-166.
https://hdl.handle.net/21.15107/rcub_vinar_7113

Popović IA, Nešić MV, Nišavić M, Petković M. Testing the best matrix/analyte combination for MALDI TOF mass spectrometric detection of steroid hormones, amino acids, vitamins and carbohydrates. in FEBS Journal. 2016;283:166-166.
https://hdl.handle.net/21.15107/rcub_vinar_7113 .

Popović, Iva A., Nešić, Mioljub V., Nišavić, Marija, Petković, Marijana, "Testing the best matrix/analyte combination for MALDI TOF mass spectrometric detection of steroid hormones, amino acids, vitamins and carbohydrates" in FEBS Journal, 283 (2016):166-166,
https://hdl.handle.net/21.15107/rcub_vinar_7113 .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Masnikosa, Romana
AU  - Butorac, Ana
AU  - Perica, Kristina
AU  - Rilak, Ana
AU  - Korićanac, Lela
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Cindrić, Mario
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1124
AB  - Hyphenated mass spectrometry (MS) techniques have attained an important position in analysis of covalent and non-covalent interactions of metal complexes with peptides and proteins. The aim of the present study was to qualitatively and quantitatively determine ruthenium binding sites on a protein using tandem mass spectrometry and allied techniques, i.e. liquid chromatography (LC) and inductively coupled plasma optical emission spectrometry (ICP-OES). For that purpose, two newly synthesized Ru(II) complexes of a meridional geometry, namely mer-[Ru(4 Cl-tpy)(en)Cl](+) (1) and mer-[Ru(4 Cl-tpy)(dach)Cl](+) (2) (where 4 Cl-tpy = 4-chloro-2,2:6,2 -terpyridine, en = 1,2-diaminoethane and dach = 1,2-diaminocyclohexane), and bovine serum albumin were used. The binding of the complexes to the protein was investigated by means of size exclusion- and reversed phase-LC, ICP OES, matrix-assisted laser desorption ionization MS and MS/MS. Ruthenated peptide sequence and a binding target amino acid were revealed through accurate elucidation of MS/MS spectra. The results obtained in this study suggest a high binding capacity of the protein towards both complexes, with up to 5.77 +/- 0.14 and 6.95 +/- 0.43 mol of 1 and 2 bound per mol of protein, respectively. The proposed binding mechanism for the selected complexes includes the release of Cl ligand, its replacement with water molecule and further coordination to electron donor histidine residue. (C) 2016 Elsevier Inc. All rights reserved.
T2  - Journal of Inorganic Biochemistry
T1  - Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin
VL  - 159
SP  - 89
EP  - 95
DO  - 10.1016/j.jinorgbio.2016.02.034
ER  - 

@article{
author = "Nišavić, Marija and Masnikosa, Romana and Butorac, Ana and Perica, Kristina and Rilak, Ana and Korićanac, Lela and Hozić, Amela and Petković, Marijana and Cindrić, Mario",
year = "2016",
abstract = "Hyphenated mass spectrometry (MS) techniques have attained an important position in analysis of covalent and non-covalent interactions of metal complexes with peptides and proteins. The aim of the present study was to qualitatively and quantitatively determine ruthenium binding sites on a protein using tandem mass spectrometry and allied techniques, i.e. liquid chromatography (LC) and inductively coupled plasma optical emission spectrometry (ICP-OES). For that purpose, two newly synthesized Ru(II) complexes of a meridional geometry, namely mer-[Ru(4 Cl-tpy)(en)Cl](+) (1) and mer-[Ru(4 Cl-tpy)(dach)Cl](+) (2) (where 4 Cl-tpy = 4-chloro-2,2:6,2 -terpyridine, en = 1,2-diaminoethane and dach = 1,2-diaminocyclohexane), and bovine serum albumin were used. The binding of the complexes to the protein was investigated by means of size exclusion- and reversed phase-LC, ICP OES, matrix-assisted laser desorption ionization MS and MS/MS. Ruthenated peptide sequence and a binding target amino acid were revealed through accurate elucidation of MS/MS spectra. The results obtained in this study suggest a high binding capacity of the protein towards both complexes, with up to 5.77 +/- 0.14 and 6.95 +/- 0.43 mol of 1 and 2 bound per mol of protein, respectively. The proposed binding mechanism for the selected complexes includes the release of Cl ligand, its replacement with water molecule and further coordination to electron donor histidine residue. (C) 2016 Elsevier Inc. All rights reserved.",
journal = "Journal of Inorganic Biochemistry",
title = "Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin",
volume = "159",
pages = "89-95",
doi = "10.1016/j.jinorgbio.2016.02.034"
}

Nišavić, M., Masnikosa, R., Butorac, A., Perica, K., Rilak, A., Korićanac, L., Hozić, A., Petković, M.,& Cindrić, M.. (2016). Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin. in Journal of Inorganic Biochemistry, 159, 89-95.
https://doi.org/10.1016/j.jinorgbio.2016.02.034

Nišavić M, Masnikosa R, Butorac A, Perica K, Rilak A, Korićanac L, Hozić A, Petković M, Cindrić M. Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin. in Journal of Inorganic Biochemistry. 2016;159:89-95.
doi:10.1016/j.jinorgbio.2016.02.034 .

Nišavić, Marija, Masnikosa, Romana, Butorac, Ana, Perica, Kristina, Rilak, Ana, Korićanac, Lela, Hozić, Amela, Petković, Marijana, Cindrić, Mario, "Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin" in Journal of Inorganic Biochemistry, 159 (2016):89-95,
https://doi.org/10.1016/j.jinorgbio.2016.02.034 . .

TY  - JOUR
AU  - Butorac, Ana
AU  - Mekic, Meliha Solak
AU  - Hozić, Amela
AU  - Diminic, Janko
AU  - Gamberger, Dragan
AU  - Nišavić, Marija
AU  - Cindrić, Mario
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1183
AB  - RATIONALE: One of the most challenging tasks of proteomics is peptide de novo sequencing. 4-Sulfophenyl isothiocyanate (SPITC) peptide derivatization enables acquisition of high-quality tandem mass spectra (MS/MS) for de novo sequencing, but unwanted non-specific reactions and reduced mass spectra (MS) signal intensities still represent the obstacles in highthroughput de novo sequencing. METHODS: We developed a SPITC peptide derivatization procedure under acidic conditions (pH LT = 5). Derivatized peptides were analyzed by matrix-assisted laser desorption/ionization (MALDI-MS) in negative ion mode followed by MS/MS in positive ion mode. A de novo sequencing tool, named DUST, adjusted to SPITC chemistry, was designed for successful high-throughput peptide de novo sequencing. This high-throughput peptide de novo sequencing was tested on Fusarium delphinoides, an organism with an uncharacterized genome. RESULTS: The SPITC derivatization procedure under acidic conditions produced a significantly improved MS dataset in comparison to commonly used derivatization under basic conditions. Signal intensities were 6 to 10 times greater and the over-sulfonation effect measured on lysine-containing peptides was significantly decreased. Furthermore, development of a novel DUST algorithm enabled automated de novo sequencing with the calculated accuracy of 70.6%. CONCLUSIONS: The SPITC derivatization and de novo sequencing approach outlined here provides a reliable method for high-throughput peptide de novo sequencing. High-throughput peptide de novo sequencing enabled protein mutation identification and identification of proteins from organisms with non-sequenced genomes. Copyright (C) 2016 John Wiley and Sons, Ltd.
T2  - Rapid Communications in Mass Spectrometry
T1  - Benefits of selective peptide derivatization with sulfonating reagent at acidic pH for facile matrix-assisted laser desorption/ionization de novo sequencing
VL  - 30
IS  - 14
SP  - 1687
EP  - 1694
DO  - 10.1002/rcm.7594
ER  - 

@article{
author = "Butorac, Ana and Mekic, Meliha Solak and Hozić, Amela and Diminic, Janko and Gamberger, Dragan and Nišavić, Marija and Cindrić, Mario",
year = "2016",
abstract = "RATIONALE: One of the most challenging tasks of proteomics is peptide de novo sequencing. 4-Sulfophenyl isothiocyanate (SPITC) peptide derivatization enables acquisition of high-quality tandem mass spectra (MS/MS) for de novo sequencing, but unwanted non-specific reactions and reduced mass spectra (MS) signal intensities still represent the obstacles in highthroughput de novo sequencing. METHODS: We developed a SPITC peptide derivatization procedure under acidic conditions (pH LT = 5). Derivatized peptides were analyzed by matrix-assisted laser desorption/ionization (MALDI-MS) in negative ion mode followed by MS/MS in positive ion mode. A de novo sequencing tool, named DUST, adjusted to SPITC chemistry, was designed for successful high-throughput peptide de novo sequencing. This high-throughput peptide de novo sequencing was tested on Fusarium delphinoides, an organism with an uncharacterized genome. RESULTS: The SPITC derivatization procedure under acidic conditions produced a significantly improved MS dataset in comparison to commonly used derivatization under basic conditions. Signal intensities were 6 to 10 times greater and the over-sulfonation effect measured on lysine-containing peptides was significantly decreased. Furthermore, development of a novel DUST algorithm enabled automated de novo sequencing with the calculated accuracy of 70.6%. CONCLUSIONS: The SPITC derivatization and de novo sequencing approach outlined here provides a reliable method for high-throughput peptide de novo sequencing. High-throughput peptide de novo sequencing enabled protein mutation identification and identification of proteins from organisms with non-sequenced genomes. Copyright (C) 2016 John Wiley and Sons, Ltd.",
journal = "Rapid Communications in Mass Spectrometry",
title = "Benefits of selective peptide derivatization with sulfonating reagent at acidic pH for facile matrix-assisted laser desorption/ionization de novo sequencing",
volume = "30",
number = "14",
pages = "1687-1694",
doi = "10.1002/rcm.7594"
}

Butorac, A., Mekic, M. S., Hozić, A., Diminic, J., Gamberger, D., Nišavić, M.,& Cindrić, M.. (2016). Benefits of selective peptide derivatization with sulfonating reagent at acidic pH for facile matrix-assisted laser desorption/ionization de novo sequencing. in Rapid Communications in Mass Spectrometry, 30(14), 1687-1694.
https://doi.org/10.1002/rcm.7594

Butorac A, Mekic MS, Hozić A, Diminic J, Gamberger D, Nišavić M, Cindrić M. Benefits of selective peptide derivatization with sulfonating reagent at acidic pH for facile matrix-assisted laser desorption/ionization de novo sequencing. in Rapid Communications in Mass Spectrometry. 2016;30(14):1687-1694.
doi:10.1002/rcm.7594 .

Butorac, Ana, Mekic, Meliha Solak, Hozić, Amela, Diminic, Janko, Gamberger, Dragan, Nišavić, Marija, Cindrić, Mario, "Benefits of selective peptide derivatization with sulfonating reagent at acidic pH for facile matrix-assisted laser desorption/ionization de novo sequencing" in Rapid Communications in Mass Spectrometry, 30, no. 14 (2016):1687-1694,
https://doi.org/10.1002/rcm.7594 . .

TY  - JOUR
AU  - Popović, Iva A.
AU  - Nešić, Maja D.
AU  - Nišavić, Marija
AU  - Vranješ, Mila
AU  - Radetić, Tamara
AU  - Šaponjić, Zoran
AU  - Masnikosa, Romana
AU  - Petković, Marijana
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/544
AB  - Nanostructured materials as substrates for surface-assisted laser desorption and ionization time-of-flight mass spectrometry have two main advantages such as small number of signals in the low mass range and salt tolerance. We have also previously observed decreased extent of undesired fragmentation of bipyridine-containing transition metal complexes in the presence of TiO2 nanoparticles (NPs). In this work, we extended our previous study and tested whether both TiO2 NPs and TiO2 prolate nanospheroids (PNSs) can be used as substrates for SALDI-MS of bipyridine-containing transition metal complexes and whether they tolerate intense laser and the presence of inorganic salts. TiO2 NPs (an average diameter of 5 nm) and PNSs (length: 40-50 nm, the lateral dimension: 14-16 nm) were characterized microscopically and their mass spectra were analyzed, as well as the spectra of bipyridine-containing Pt(II) and Ru(III) complexes. Our results show that seven times higher analyte signals can be obtained in the presence of PNSs compared to the signals acquired with NPs and three times higher compared to spectra acquired without a substrate. The presence of inorganic salt did not affect the spectra, which makes both TiO2 nanocrystals suitable for MS analysis of transition metal complexes in biological fluids. (C) 2015 Elsevier B.V. All rights reserved.
T2  - Materials Letters
T1  - Suitability of TiO2 nanoparticles and prolate nanospheroids for laser desorption/ionization mass spectrometric characterization of bipyridine-containing complexes
VL  - 150
SP  - 84
EP  - 88
DO  - 10.1016/j.matlet.2015.03.004
ER  - 

@article{
author = "Popović, Iva A. and Nešić, Maja D. and Nišavić, Marija and Vranješ, Mila and Radetić, Tamara and Šaponjić, Zoran and Masnikosa, Romana and Petković, Marijana",
year = "2015",
abstract = "Nanostructured materials as substrates for surface-assisted laser desorption and ionization time-of-flight mass spectrometry have two main advantages such as small number of signals in the low mass range and salt tolerance. We have also previously observed decreased extent of undesired fragmentation of bipyridine-containing transition metal complexes in the presence of TiO2 nanoparticles (NPs). In this work, we extended our previous study and tested whether both TiO2 NPs and TiO2 prolate nanospheroids (PNSs) can be used as substrates for SALDI-MS of bipyridine-containing transition metal complexes and whether they tolerate intense laser and the presence of inorganic salts. TiO2 NPs (an average diameter of 5 nm) and PNSs (length: 40-50 nm, the lateral dimension: 14-16 nm) were characterized microscopically and their mass spectra were analyzed, as well as the spectra of bipyridine-containing Pt(II) and Ru(III) complexes. Our results show that seven times higher analyte signals can be obtained in the presence of PNSs compared to the signals acquired with NPs and three times higher compared to spectra acquired without a substrate. The presence of inorganic salt did not affect the spectra, which makes both TiO2 nanocrystals suitable for MS analysis of transition metal complexes in biological fluids. (C) 2015 Elsevier B.V. All rights reserved.",
journal = "Materials Letters",
title = "Suitability of TiO2 nanoparticles and prolate nanospheroids for laser desorption/ionization mass spectrometric characterization of bipyridine-containing complexes",
volume = "150",
pages = "84-88",
doi = "10.1016/j.matlet.2015.03.004"
}

Popović, I. A., Nešić, M. D., Nišavić, M., Vranješ, M., Radetić, T., Šaponjić, Z., Masnikosa, R.,& Petković, M.. (2015). Suitability of TiO2 nanoparticles and prolate nanospheroids for laser desorption/ionization mass spectrometric characterization of bipyridine-containing complexes. in Materials Letters, 150, 84-88.
https://doi.org/10.1016/j.matlet.2015.03.004

Popović IA, Nešić MD, Nišavić M, Vranješ M, Radetić T, Šaponjić Z, Masnikosa R, Petković M. Suitability of TiO2 nanoparticles and prolate nanospheroids for laser desorption/ionization mass spectrometric characterization of bipyridine-containing complexes. in Materials Letters. 2015;150:84-88.
doi:10.1016/j.matlet.2015.03.004 .

Popović, Iva A., Nešić, Maja D., Nišavić, Marija, Vranješ, Mila, Radetić, Tamara, Šaponjić, Zoran, Masnikosa, Romana, Petković, Marijana, "Suitability of TiO2 nanoparticles and prolate nanospheroids for laser desorption/ionization mass spectrometric characterization of bipyridine-containing complexes" in Materials Letters, 150 (2015):84-88,
https://doi.org/10.1016/j.matlet.2015.03.004 . .

TY  - JOUR
AU  - Radisavljevic, Maja
AU  - Kamceva, Tina
AU  - Vukićević, Iva A.
AU  - Nišavić, Marija
AU  - Milovanović, Milan
AU  - Petković, Marijana
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5605
AB  - We compare the quality and reliability of laser desorption and ionisation mass spectra of FeCl3 acquired without the assistance of the matrix with the spectra acquired with different organic matrix molecules. Generally, inorganic salts tend to form clusters upon laser irradiation, the signals of which can be easily distinguished from ions arising from the matrix. In the presence of a matrix, cluster ions are, however, mostly suppressed. We have compared the number of analyte signals, accuracy of determination of isotope composition of the analyte and the sensitivity of FeCl3 detection between different approaches. The results obtained imply that the sensitivity of mass spectrometric analysis of FeCl3 is somewhat higher when matrices are applied than in the matrix-free approach. Among all matrices tested in this work, F20TPP seems to be the most promising for further applications as a matrix for mass spectrometry of inorganic salts.
T2  - European Journal of Mass Spectrometry
T1  - Sensitivity and accuracy of organic matrix-assisted Laser desorption and ionisation mass spectrometry of FeCl3 is higher than in in matrix-free approach
VL  - 19
IS  - 2
SP  - 77
EP  - 89
DO  - 10.1255/ejms.1217
ER  - 

@article{
author = "Radisavljevic, Maja and Kamceva, Tina and Vukićević, Iva A. and Nišavić, Marija and Milovanović, Milan and Petković, Marijana",
year = "2013",
abstract = "We compare the quality and reliability of laser desorption and ionisation mass spectra of FeCl3 acquired without the assistance of the matrix with the spectra acquired with different organic matrix molecules. Generally, inorganic salts tend to form clusters upon laser irradiation, the signals of which can be easily distinguished from ions arising from the matrix. In the presence of a matrix, cluster ions are, however, mostly suppressed. We have compared the number of analyte signals, accuracy of determination of isotope composition of the analyte and the sensitivity of FeCl3 detection between different approaches. The results obtained imply that the sensitivity of mass spectrometric analysis of FeCl3 is somewhat higher when matrices are applied than in the matrix-free approach. Among all matrices tested in this work, F20TPP seems to be the most promising for further applications as a matrix for mass spectrometry of inorganic salts.",
journal = "European Journal of Mass Spectrometry",
title = "Sensitivity and accuracy of organic matrix-assisted Laser desorption and ionisation mass spectrometry of FeCl3 is higher than in in matrix-free approach",
volume = "19",
number = "2",
pages = "77-89",
doi = "10.1255/ejms.1217"
}

Radisavljevic, M., Kamceva, T., Vukićević, I. A., Nišavić, M., Milovanović, M.,& Petković, M.. (2013). Sensitivity and accuracy of organic matrix-assisted Laser desorption and ionisation mass spectrometry of FeCl3 is higher than in in matrix-free approach. in European Journal of Mass Spectrometry, 19(2), 77-89.
https://doi.org/10.1255/ejms.1217

Radisavljevic M, Kamceva T, Vukićević IA, Nišavić M, Milovanović M, Petković M. Sensitivity and accuracy of organic matrix-assisted Laser desorption and ionisation mass spectrometry of FeCl3 is higher than in in matrix-free approach. in European Journal of Mass Spectrometry. 2013;19(2):77-89.
doi:10.1255/ejms.1217 .

Radisavljevic, Maja, Kamceva, Tina, Vukićević, Iva A., Nišavić, Marija, Milovanović, Milan, Petković, Marijana, "Sensitivity and accuracy of organic matrix-assisted Laser desorption and ionisation mass spectrometry of FeCl3 is higher than in in matrix-free approach" in European Journal of Mass Spectrometry, 19, no. 2 (2013):77-89,
https://doi.org/10.1255/ejms.1217 . .