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A Weakly Clustered N terminus Inhibits Aβ(1–40) Amyloidogenesis
Author(s) -
Lim Kwang Hun
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600270
Subject(s) - chemistry , peptide , n terminus , c terminus , amyloid (mycology) , biochemistry , computational biology , stereochemistry , biophysics , amino acid , peptide sequence , biology , gene , inorganic chemistry
Take pills for stability? A partly structured N terminus was detected in the β‐amyloid (1–40) peptide by using dynamic NMR studies. This partly clustered N terminus (residues 5–16; shown here) was disrupted under amyloidogenic conditions (high temperature, low pH, and in the presence of Zn 2+ ions). The results suggest that destabilization of this cluster might be a key step in Aβ amyloidogenesis.