High-Efficiency Microflow and Nanoflow Negative Electrospray Ionization of Peptides Induced by Gas-Phase Proton Transfer Reactions
Samo za registrovane korisnike
2017
Autori
Nišavić, MarijaHozić, Amela
Hameršak, Zdenko
Radić, Martina
Butorac, Ana
Duvnjak, Marija
Cindrić, Mario
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 nega...tively 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.
Izvor:
Analytical Chemistry, 2017, 89, 9, 4847-4854Finansiranje / projekti:
- Ispitivanje mehanizma reakcija kompleksa jona prelaznih metala sa biološki značajnim molekulima (RS-172011)
- SIIF project ApliMetaFarma [RC.2.2.08-0046]
- HrZZ project [PEPTGLYCOSAR IP-2014-09-7899]
DOI: 10.1021/acs.analchem.6b04466
ISSN: 0003-2700; 1520-6882
PubMed: 28372357
WoS: 000400723600015
Scopus: 2-s2.0-85020746493
Kolekcije
Institucija/grupa
VinčaTY - 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 . .