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

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry
Original language description
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
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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