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Nat Chem Biol. 2008 Mar;4(3):197-9. doi: 10.1038/nchembio.65. Epub 2008 Jan 27.

Small-molecule aggregates inhibit amyloid polymerization.

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  • 1Department of Pharmaceutical Chemistry and Graduate Group in Chemistry and Chemical Biology, University of California San Francisco, 1700 4th Street, San Francisco, California 94158-2330, USA.

Abstract

Many amyloid inhibitors resemble molecules that form chemical aggregates, which are known to inhibit many proteins. Eight known chemical aggregators inhibited amyloid formation of the yeast and mouse prion proteins Sup35 and recMoPrP in a manner characteristic of colloidal inhibition. Similarly, three known anti-amyloid molecules inhibited beta-lactamase in a detergent-dependent manner, which suggests that they too form colloidal aggregates. The colloids localized to preformed fibers and prevented new fiber formation in electron micrographs. They also blocked infection of yeast cells with Sup35 prions, which suggests that colloidal inhibition may be relevant in more biological milieus.

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PMID:
18223646
[PubMed - indexed for MEDLINE]
PMCID:
PMC2730835
Free PMC Article

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