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 heterogeneity and metastable nature. A better understanding of Aβ species’ assembly details and structural properties has been more characterized recently. Numerous potential inhibitors have been identified that they can effectively bind to 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.
Keywords: Alzheimer's disease, Aβ species, conformational structure, Aβ inhibitors, computational approach, molecular simulations.
Current Pharmaceutical Design
Title:Understanding the Binding Mechanism of Amyloid-β Inhibitors from Molecular Simulations
Volume: 24 Issue: 28
Author(s): Linh Tran*
Affiliation:
- Computational Chemistry Research Group, Ton Duc Thang University, Ho Chi Minh, City,Vietnam
Keywords: Alzheimer's disease, Aβ species, conformational structure, Aβ inhibitors, computational approach, molecular simulations.
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 heterogeneity and metastable nature. A better understanding of Aβ species’ assembly details and structural properties has been more characterized recently. Numerous potential inhibitors have been identified that they can effectively bind to 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.
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Cite this article as:
Tran Linh *, Understanding the Binding Mechanism of Amyloid-β Inhibitors from Molecular Simulations, Current Pharmaceutical Design 2018; 24 (28) . https://dx.doi.org/10.2174/1381612824666180813093420
DOI https://dx.doi.org/10.2174/1381612824666180813093420 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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