...
首页> 外文期刊>Journal of Proteins and Proteomics >Wine-related flavonols for therapeutic use in Alzheimer’s disease, an in-silico investigation
【24h】

Wine-related flavonols for therapeutic use in Alzheimer’s disease, an in-silico investigation

机译:

获取原文
           

摘要

Abstract The aggregation of amyloid-β (Aβ) peptides into decrepit plaques is distinctive of Alzheimer’s disease (AD). Aggregated Aβ fibrils are neurotoxic to the brain. This deposition of aggregates is central to AD-related neurodegeneration. Conforming to literature, amino acid residues KLVFF (16–20) in the Aβ monomer self-associate to form antiparallel β-sheet fibrils. Small molecules binding to the Aβ16–20 regions of Aβ42 can inhibit the self-assembly and disrupt Aβ fibril. Naturally occurring flavonols have shown the potential to inhibit protein aggregates found in AD. Present work investigated flavonols in complex with amyloid monomer, Aβm, and amyloid fibril Aβf using docking, followed by 100 ns molecular dynamics simulation (MDS) of the best docked Aβm-flavonol and Aβf-flavonol complexes. Molecular Mechanics Poisson–Boltzmann Surface Area (MMPBSA) method estimated the binding free energy of these complexes from MDS trajectories. These in-silico methods provided atomistic-detailed information about the binding and inhibitory properties of the selected wine-related flavonols, kaempferol (KAE), myricetin (MYR), morin (MOR), and quercetin (QUE). This selection of the flavonols was based on the structural variations in the number and placement of hydroxyl groups on the flavonoid backbone. These flavonols interacted with the residues in the hydrophobic region (Lys16 to Ala21) of the Aβm and Aβf to form complexes.

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号