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

0189355 - UMCH-V 20033310 RIV NL eng J - Journal Article
Strohalm, M. - Kodíček, M. - Pechar, Michal
Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry.
Biochemical and Biophysical Research Communications. Roč. 312, č. 3 (2003), s. 811-816. ISSN 0006-291X. E-ISSN 1090-2104
R&D Projects: GA ČR GA203/02/0922; GA AV ČR KSK4055109
Institutional research plan: CEZ:AV0Z4050913
Keywords : MALDI-TOF mass spectrometry * 2-hydroxy-5-nitrobenzyl bromide * Koshland reagent
Subject RIV: CE - Biochemistry
Impact factor: 2.836, year: 2003

The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) is a common covalent modification of tryptophan. It results in several products which have been described by classical physico-chemical methods. To improve the understanding of the HNB-modified tryptophan structure, we synthesized a model peptide containing one tryptophan only, modified it by HNB, and analyzed the product by MALDI-TOF mass spectrometry. Surprisingly, several multi-modified products (up to 5 HNB moieties per one tryptophan) were identified.
Permanent Link: http://hdl.handle.net/11104/0085176