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 Lettjournal_title
FEBS lettersauthors
Abelein A,Lang L,Lendel C,Gräslund A,Danielsson Jdoi
10.1016/j.febslet.2012.09.035subject
Has Abstractpub_date
2012-11-16 00:00:00pages
3991-5issue
22eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00757-0journal_volume
586pub_type
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