Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008980" target="_blank" >RIV/60461373:22330/03:00008980 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry

Popis výsledku v původním jazyce

The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) is a common covalent modification of tryptophan. It results in several products which were described by classical physico-chemical methods. For better understanding the structure of HNB-modified tryptophan, we synthesized a model peptide containing only one tryptophan, modified it by HNB and analyzed the product by MALDI-TOF mass spectrometry. Several multi-modified products (up to 5 HNB moieties per one tryptophan) were identified, surprisingly. An influence of HNB concentration and pH on a degree of modification was also analyzed. In addition, a splitting of modified tryptophan peaks in MALDI-TOF spectrum was detected; most probably, this effect is a common MALDI artifact of nitro-aromatic compounds which can make identification of HNB-modified tryptophan by MALDI-TOF MS very simple

Název v anglickém jazyce

Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry

Popis výsledku anglicky

The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) is a common covalent modification of tryptophan. It results in several products which were described by classical physico-chemical methods. For better understanding the structure of HNB-modified tryptophan, we synthesized a model peptide containing only one tryptophan, modified it by HNB and analyzed the product by MALDI-TOF mass spectrometry. Several multi-modified products (up to 5 HNB moieties per one tryptophan) were identified, surprisingly. An influence of HNB concentration and pH on a degree of modification was also analyzed. In addition, a splitting of modified tryptophan peaks in MALDI-TOF spectrum was detected; most probably, this effect is a common MALDI artifact of nitro-aromatic compounds which can make identification of HNB-modified tryptophan by MALDI-TOF MS very simple

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Studium konformace bílkovin pomocí hmotnostní spektrometrie na principu MALDI-TOF (Matrix Assisted Laser Desorption Ionisation - Time Of Flight)</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název periodika

Biochemical and Biophysical Research Communications

ISSN

0006-291X

e-ISSN

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Svazek periodika

2003

Číslo periodika v rámci svazku

312

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

6

Strana od-do

811-816

Kód UT WoS článku

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EID výsledku v databázi Scopus

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