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Isomerization of the Asp7 Residue Results in Zinc‐Induced Oligomerization of Alzheimer’s Disease Amyloid β(1–16) Peptide
Author(s) -
Tsvetkov Philipp O.,
Popov Igor A.,
Nikolaev Eugene N.,
Archakov Alexander I.,
Makarov Alexander A.,
Kozin Sergey A.
Publication year - 2008
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.200700784
Subject(s) - chemistry , peptide , isomerization , asparagine , residue (chemistry) , amyloid (mycology) , alzheimer's disease , zinc , biochemistry , biophysics , disease , biology , medicine , enzyme , catalysis , inorganic chemistry , organic chemistry
One small change : Isomerization of Asp7, the most abundant naturally occurring post‐translational modification in Alzheimer's disease (AD) amyloid‐β peptide (Aβ), causes zinc‐induced oligomerization of the Aβ zinc‐binding domain and could play a triggering role in pathology onset. Substitution of Asp7 by Asn in Aβ (the Tottori–Japan mutation) might also be significant, since asparagine is known to be much more susceptible than aspartate to spontaneous conversion into isoaspartate.