Abstract

Small organic molecules, like Congo red and lacmoid, have been shown to modulate the self-assembly of the amyloid beta peptide (A beta). Here, we show that A beta 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 A beta is in the co-aggregate. These weak transient interactions kinetically redirect the aggregation prone A beta from self-assembling into amyloid fibrils. These findings suggest that even such weak binders might be effective as therapeutics against pathogenic protein aggregation. (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Keywords

Amyloid; Alzheimer's disease; NMR relaxation dispersion; Dynamic exchange

Published in

FEBS Letters
2012, Volume: 586, number: 22, pages: 3991-3995
Publisher: ELSEVIER SCIENCE BV

SLU Authors

• Lendel, Christofer

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Biochemistry and Molecular Biology
Biophysics


Publication identifier

DOI: https://doi.org/10.1016/j.febslet.2012.09.035

Permanent link to this page (URI)

https://res.slu.se/id/publ/41040