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European Union REGIONAL COMPETITIVENESS ApliMetaFarma [RC.2.2.08-0046]

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Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin

Nišavić, Marija; Masnikosa, Romana; Butorac, Ana; Perica, Kristina; Rilak, Ana; Korićanac, Lela; Hozić, Amela; Petković, Marijana; Cindrić, Mario

(2016)

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 . .
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