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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Abelein A,Lang L,Lendel C,Gräslund A,Danielsson J

doi

10.1016/j.febslet.2012.09.035

subject

Has Abstract

pub_date

2012-11-16 00:00:00

pages

3991-5

issue

22

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00757-0

journal_volume

586

pub_type

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