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The Aggregated State of Amyloid‐β Peptide In Vitro Depends on Cu<sup>2+</sup> Ion Concentration
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Citations
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References
2007
Year
Colloidal MaterialEngineeringVitro DependsAggregated Amyloid-β DependsPeptide ScienceProtein Phase SeparationChemistryAggregated StateAmyloid‐β PeptideProtein FoldingProtein MisfoldingBiophysicsBiochemistryColloidal PropertyPhysical ChemistryCrystallographyColloidal SystemElectron Spin ResonanceCu2+ IonsMedicine
Hold them or fold them: The morphology of aggregated amyloid-β depends on the concentration of Cu2+ ions, as shown in the TEM images. Distinct differences in the coordination of Cu2+ ions to amyloid-β are observed by electron spin resonance as the metal concentration increases. The results suggest a correlation between specific Cu2+ ion coordination and the overall morphology of aggregates. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z700318_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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