Premium
The Aggregated State of Amyloid‐β Peptide In Vitro Depends on Cu 2+ Ion Concentration
Author(s) -
Jun Sangmi,
Saxena Sunil
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700318
Subject(s) - electron paramagnetic resonance , ion , amyloid (mycology) , in vitro , chemistry , peptide , metal ions in aqueous solution , metal , crystallography , biophysics , biochemistry , nuclear magnetic resonance , inorganic chemistry , physics , biology , organic chemistry
Hold them or fold them : The morphology of aggregated amyloid‐β depends on the concentration of Cu 2+ ions, as shown in the TEM images. Distinct differences in the coordination of Cu 2+ ions to amyloid‐β are observed by electron spin resonance as the metal concentration increases. The results suggest a correlation between specific Cu 2+ ion coordination and the overall morphology of aggregates.