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On‐line high‐performance liquid chromatography/mass spectrometric investigation of amyloid‐β peptide variants found in Alzheimer's disease
Author(s) -
Thompson Andrew J.,
Lim Teck K.,
Barrow Colin J.
Publication year - 1999
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/(sici)1097-0231(19991215)13:23<2348::aid-rcm797>3.0.co;2-j
Subject(s) - chemistry , pathogenesis , peptide , high performance liquid chromatography , mass spectrometry , chromatography , amyloid (mycology) , electrospray ionization , alzheimer's disease , amyloid β , disease , biochemistry , medicine , inorganic chemistry
Aβ peptides are the major components of amyloid deposits in Alzheimer's disease. The presence of N‐terminally truncated Aβ variants in amyloid may be a critical factor in Alzheimer's disease pathogenesis. These Aβ variants are less soluble and more amyloidogenic than full‐length Aβ, making their separation, purification and identification difficult. High‐performance liquid chromatography (HPLC) at elevated temperatures, coupled to electrospray ionization (ES) mass spectrometry (MS), enables rapid separation and identification of N‐terminally truncated Aβ variants. This methodology provides a potential tool for exploring the importance of these Aβ variants in both the pathogenesis and diagnosis of Alzheimer's disease. Copyright © 1999 John Wiley & Sons, Ltd.