Disulfide bond decay during matrix-assisted laser desorption/ionization time-of-flight mass spectrometry experiments

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F11%3A43891997" target="_blank" >RIV/60461373:22330/11:43891997 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/rcm.5140" target="_blank" >http://dx.doi.org/10.1002/rcm.5140</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/rcm.5140" target="_blank" >10.1002/rcm.5140</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Disulfide bond decay during matrix-assisted laser desorption/ionization time-of-flight mass spectrometry experiments

Popis výsledku v původním jazyce

In our laboratory, we have been studying the reductive processes that occur during matrix-assisted laser desorption/ionization (MALDI) experiments. Recently, we have finished an analysis of the DHB matrix effect on the azo group in cyclic peptides. However, deep understanding of disulfide bond behaviour during a mass spectrometry (MS) experiment is much more important in proteomics as its reduction can cause serious errors in protein spectra interpretation. Therefore, we have focused on Intra- and intermolecular disulfide bonds as well as disulfide bonds connecting cysteine and 2-thio-5-nitrobenzoic acid (TNB, Ellman's reagent modification) in model peptides during MALDI MS measurements. While the reduction was not observed for Intra- and intermolecular cysteine-cysteine disulfide bonds, the disulfide connection between cysteine and TNB was always affected. It was proved that TNB and Ellman's reagent can act as a matrix itself. The results obtained enabled us to propose a reaction mech

Název v anglickém jazyce

Disulfide bond decay during matrix-assisted laser desorption/ionization time-of-flight mass spectrometry experiments

Popis výsledku anglicky

In our laboratory, we have been studying the reductive processes that occur during matrix-assisted laser desorption/ionization (MALDI) experiments. Recently, we have finished an analysis of the DHB matrix effect on the azo group in cyclic peptides. However, deep understanding of disulfide bond behaviour during a mass spectrometry (MS) experiment is much more important in proteomics as its reduction can cause serious errors in protein spectra interpretation. Therefore, we have focused on Intra- and intermolecular disulfide bonds as well as disulfide bonds connecting cysteine and 2-thio-5-nitrobenzoic acid (TNB, Ellman's reagent modification) in model peptides during MALDI MS measurements. While the reduction was not observed for Intra- and intermolecular cysteine-cysteine disulfide bonds, the disulfide connection between cysteine and TNB was always affected. It was proved that TNB and Ellman's reagent can act as a matrix itself. The results obtained enabled us to propose a reaction mech

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Rapid Communications in Mass Spectrometry

ISSN

0951-4198

e-ISSN

—

Svazek periodika

25

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

2468-2474

Kód UT WoS článku

000294267200014

EID výsledku v databázi Scopus

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