Journal
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
Volume 15, Issue 10, Pages 5169-5174Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jctc.9b00599
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Funding
- National Institutes of Health [GM114300]
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Aggregation of amyloid-beta (A beta) peptides is a crucial step in the progression of Alzheimer's disease (AD). Identifying aggregation inhibitors against AD has been a great challenge. We report an atomistic simulation study of the inhibition mechanism of two small molecules, homotaurine and scyllo-inositol, which are AD drug candidates currently under investigation. We show that both small molecules promote a conformational change of the A beta 42 monomer toward a more collapsed phase through a nonspecific binding mechanism. This finding provides atomistic-level insights into designing potential drug candidates for future AD treatments.
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