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Characterization of intermolecular β‐sheet peptides by mass spectrometry and hydrogen isotope exchange
Author(s) -
Kraus Mario,
Janek Katharina,
Bienert Michael,
Krause Eberhard
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20000715)14:13<1094::aid-rcm994>3.0.co;2-5
Subject(s) - chemistry , hydrogen–deuterium exchange , mass spectrometry , beta sheet , electrospray ionization , deuterium , intermolecular force , dissociation (chemistry) , hydrogen , protein mass spectrometry , peptide , fragmentation (computing) , analytical chemistry (journal) , crystallography , chromatography , molecule , organic chemistry , biochemistry , physics , quantum mechanics , computer science , operating system
The self‐assembly of β‐sheet peptide domains resulting in the formation of fibrillar aggregates (amyloids) is a feature of various neurodegenerative disorders. In order to evaluate mass spectrometric methods for the characterization of intermolecular β‐sheet structures the hydrogen/deuterium exchange behaviour of model peptides DPKGDPKG‐(VT) n ‐GKGDPKPD‐amide (n = 3,4,5,6,7,8), (VT) n ‐peptides, composed of a central β‐sheet‐forming domain and N‐ and C‐terminal nonstructured octapeptide sequences, was measured by electrospray ionization mass spectrometry (ESI‐MS) and matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS). The kinetic analysis of the hydrogen/deuterium exchange (HX) shows that intermolecular β‐sheet structures contain slowly exchanging protons (k ≤0.001 1/min). Localization of β‐sheet domains was achieved by monitoring the hydrogen exchange of peptide fragments generated via collision‐induced dissociation (CID) or post source decay (PSD). The hydrogen exchange kinetics and the β‐sheet domains determined by ESI‐ and MALDI‐MS were found to correlate with the length and stability of the β‐structure domain of the (VT) n ‐peptides. Copyright © 2000 John Wiley & Sons, Ltd.