Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
14680838
DOI
10.1016/j.bbrc.2003.11.004
PII: S0006291X03023349
Knihovny.cz E-zdroje
- MeSH
- 2-hydroxy-5-nitrobenzylbromid chemie MeSH
- koncentrace vodíkových iontů MeSH
- makromolekulární látky MeSH
- peptidové fragmenty MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice metody MeSH
- tryptofan analogy a deriváty chemická syntéza chemie MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 2-hydroxy-5-nitrobenzylbromid MeSH
- makromolekulární látky MeSH
- peptidové fragmenty MeSH
- tryptofan MeSH
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. the influence of HNB concentration and pH on the degree of modification was also analyzed. In addition, a splitting of modified tryptophan peaks in MALDI-TOF spectrum was described; most probably, this effect is a common MALDI artifact of nitro-aromatic compounds which facilitates the identification of HNB-modified tryptophan by MALDI-TOF MS significantly.
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