The Aggregated State of Amyloid‐β Peptide In Vitro Depends on Cu 2+  Ion Concentration | Zendy

Jun Sangmi | Zendy; Saxena Sunil | Zendy

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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.

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