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Characterisation of adducts of the lipid peroxidation product 4‐hydroxy‐2‐nonenal and amyloid β‐peptides by liquid chromatography/electrospray ionisation mass spectrometry
Author(s) -
Magni F.,
Galbusera C.,
Tremolada L.,
Ferrarese C.,
Kienle M. Galli
Publication year - 2002
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/rcm.743
Subject(s) - chemistry , adduct , mass spectrometry , electrospray , peptide , electrospray ionization , lipid peroxidation , chromatography , liquid chromatography–mass spectrometry , biochemistry , antioxidant , organic chemistry
Alzheimer's disease is characterised by brain neuritic plaques composed of a 39–44 amino acid peptide (Aβ). Lipid peroxidation is an early event induced by these amyloid β‐peptides, leading to the formation of 4‐hydroxy‐2‐nonenal (HNE), which is one of the major end products of this process. HNE has been reported to form adducts via a stable covalent binding to proteins through a Michael addition to amino acid residues with a nucleophilic side chain. The present study reports an investigation of the conditions for formation of Aβ‐HNE (Aβ 1–28 and Aβ 1–42) adducts, and their characterisation by liquid chromatography/electrospray ionisation mass spectrometry (LC/ESI‐MS). The results suggest that one or more HNE moieties are localised in the 6–16 region of these adducts, while Asp‐1, Lys‐16 and Lys‐28 are not modified under the described reaction conditions. Copyright © 2002 John Wiley & Sons, Ltd.