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Peptide backbone modification in the bend region of amyloid‐ β inhibits fibrillogenesis but not oligomer formation
Author(s) -
Johnson Erik C. B.,
Lanning Jennifer D.,
Meredith Stephen C.
Publication year - 2016
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2879
Subject(s) - fibrillogenesis , oligomer , peptide , chemistry , fibril , biophysics , amyloid (mycology) , amyloid fibril , p3 peptide , amyloid β , biochemistry , alzheimer's disease , amyloid precursor protein , biology , polymer chemistry , disease , medicine , inorganic chemistry
Current evidence suggests that oligomers of the amyloid‐ β (A β ) peptide are involved in the cellular toxicity of Alzheimer's disease, yet their biophysical characterization remains difficult because of lack of experimental control over the aggregation process under relevant physiologic conditions. Here, we show that modification of the A β peptide backbone at Gly29 allows for the formation of oligomers but inhibits fibril formation at physiologic temperature and pH. Our results suggest that the putative bend region in A β is important for higher‐order aggregate formation. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.