Understanding the binding mechanism of Amyloid- β inhibitors from molecular simulations.

Understanding the binding mechanism of Amyloid-β inhibitors from molecular simulations. Curr Pharm Des. 2018 Aug 12;: Authors: Tran L Abstract In recent years, Aβ aggregation prevention, one of the most concerned strategies in drug development has been carefully assessed to treat Alzheimer's disease. Aβ peptides can transform structurally from random coil monomer into β-stranded protofibril via multiple oligomeric states. Among the various Aβ species, the identification of binding targets has been challenging due to the heterogeneousity and metastable nature. A better understanding of Aβ species' assembly details and structural properties has been more characterized recently. Numerous potential inhibitors are identified that they can effectively bind on different Aβ species such as monomer, oligomer or protofibril during the inhibition of Aβ aggregation process. This review highlights the diversity of structural ensembles of Aβ species, from monomer to protofibril forms and the specific binding targets by their potential inhibitors. Comprehending the binding mechanism of Aβ inhibitors is indispensable for searching novel drug candidates against early-stage Alzheimer's disease. PMID: 30101700 [PubMed - as supplied by publisher]
Source: Current Pharmaceutical Design - Category: Drugs & Pharmacology Authors: Tags: Curr Pharm Des Source Type: research