| Literature DB >> 29711846 |
Jin Zou1, Katsushi Kajita1, Naoki Sugimoto1.
Abstract
A distinct biochemical role of Cu2+ as an inhibitor in the aggregation of the peptide Aβ(42) in vitro was revealed by thioflavin T fluorescence assay and atomic force microscopy. The Cu2+ -Aβ(42) complex is responsible for the inhibition because it stabilizes the soluble form of Aβ(42) and controls the conformational transition ([Eq. (1)]; ki =[Aβ(42)][Cu2+ ]/[Cu2+ -Aβ(42)]).Entities:
Keywords: aggregation; copper; inhibitors; peptides
Year: 2001 PMID: 29711846 DOI: 10.1002/1521-3773(20010618)40:12<2274::AID-ANIE2274>3.0.CO;2-5
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336