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

Abelein, Axel (author)

Lang, Lisa (author)

Lendel, Christofer (author)

2012-10-09
2012
English.
In: FEBS Letters. - : Elsevier. - 0014-5793 .- 1873-3468. ; 586:22, s. 3991-3995

Related links:: https://febs.onlinel...; show more...; https://urn.kb.se/re...; https://doi.org/10.1...; show less...

Abstract Subject headings

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.

By the author/editor: Abelein, Axel; Lang, Lisa; Lendel, Christof ...; Gräslund, Astrid; Danielsson, Jens

About the subject

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Biophysics

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