Molecular insights into A[beta]42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study

• Published in: Journal of molecular recognition Vol. 30; no. 12
• Main Authors: Saini, Rajneet Kaur, Shuaib, Suniba, Goyal, Bhupesh
• Format: Journal Article
• Language: English
• Published: Nutley Wiley Subscription Services, Inc 01.12.2017
• Subjects: Agglomeration; Alzheimer's disease; Binding energy; Biocompatibility; Chains; Chemical bonds; Coils; Destabilization; Dismantling; Fluorination; Free energy; Hydrogen bonds; Molecular docking; Molecular dynamics; Molecular structure; Oligomers; Simulation; Toxicity

The aggregation of amyloid [beta]-peptide (A[beta]42) into toxic oligomers, fibrils, has been identified as a key process in Alzheimer's disease (AD) progression. The role of halogen-substituted compounds have been highlighted in the disassembly of A[beta] protofibril. However, the underlying i...