Small-molecule aggregates inhibit amyloid polymerization

Brian Y. Feng, Brandon H. Toyama, Holger Wille, David W. Colby, Sean R. Collins, Barnaby C.H. May, Stanley B. Prusiner, Jonathan Weissman, Brian K. Shoichet

Research output: Contribution to journalArticle

202 Scopus citations

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 β-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.

Original languageEnglish (US)
Pages (from-to)197-199
Number of pages3
JournalNature Chemical Biology
Volume4
Issue number3
DOIs
StatePublished - Jan 1 2008

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Feng, B. Y., Toyama, B. H., Wille, H., Colby, D. W., Collins, S. R., May, B. C. H., Prusiner, S. B., Weissman, J., & Shoichet, B. K. (2008). Small-molecule aggregates inhibit amyloid polymerization. Nature Chemical Biology, 4(3), 197-199. https://doi.org/10.1038/nchembio.65