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FEBS Lett. 2012 Nov 16;586(22):3991-5. doi: 10.1016/j.febslet.2012.09.035. Epub 2012 Oct 9.

Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly.

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Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

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  • FEBS Lett. 2013 May 2;587(9):1452.


Small organic molecules, like Congo red and lacmoid, have been shown to modulate the self-assembly of the amyloid β peptide (Aβ). Here, we show that Aβ forms NMR invisible non-toxic co-aggregates together with lacmoid as well as Congo red. We find that the interaction involves two distinct kinetic processes and at every given time point only a small fraction of Aβ is in the co-aggregate. These weak transient interactions kinetically redirect the aggregation prone Aβ from self-assembling into amyloid fibrils. These findings suggest that even such weak binders might be effective as therapeutics against pathogenic protein aggregation.

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