Comparative analysis of human and Dutch-type alzheimer β-amyloid peptides by infrared spectroscopy and circular dichroism

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DOIResolve DOI: http://doi.org/10.1006/bbrc.1993.1207
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TypeArticle
Journal titleBiochemical and Biophysical Research Communications
ISSN0006-291X
Volume191
Issue1
Pages232239; # of pages: 8
AbstractThe 42 amino acid βA4 peptide is the major constituent of the senile plaques, one of the hallmark neuropathological lesions of Alzheimer′s disease. While C-terminally truncated variants were shown to be present in normal body fluids, a single Glu → Gln change in the 39 amino acid form of βA4 results in accelerated fibril formation in the brains of patients with Dutch-type hereditary cerebral hemorrhage with amyloidosis. In this study we used Fourier-transform infrared and circular dichroism spectroscopies on synthetic peptides to demonstrate that this mutation results in altered secondary structure in membrane mimicking solvents, characterized by a considerably higher β-structure content for the mutant peptide. Moreover, extreme high and low pH were less effective in eliminating the β-conformation for the Dutch-variant than for the normal human sequence.
Publication date
PublisherAcademic Press Inc.
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada
Peer reviewedYes
NRC number27
NPARC number9148095
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Record identifier370628e5-176b-40f9-a26c-b5ef69eecc62
Record created2009-06-25
Record modified2016-12-12
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