Effect of β-cyclodextrin-EGCG complexion against aggregated a-synuclein through density functional theory and discrete molecular dynamics
E Srinivasan, R Rajasekaran - Chemical Physics Letters, 2019 - Elsevier
Misfolding and aggregation of a-synuclein (AS) protein are considered to be causative
factors for Parkinson's disease. Herein, we describe molecular dynamics simulations of
aggregated AS with βC-EGCG to better characterize the detailed conformational effects on
their inhibitory action. Our results indicate that the binding of βC-EGCG disrupt the β-sheet of
aggregated AS structure and cause impairment of intermolecular interactions. Furthermore,
the free energy landscape portrayed the effect of βC-EGCG directly impedes the formation of …
factors for Parkinson's disease. Herein, we describe molecular dynamics simulations of
aggregated AS with βC-EGCG to better characterize the detailed conformational effects on
their inhibitory action. Our results indicate that the binding of βC-EGCG disrupt the β-sheet of
aggregated AS structure and cause impairment of intermolecular interactions. Furthermore,
the free energy landscape portrayed the effect of βC-EGCG directly impedes the formation of …
以上显示的是最相近的搜索结果。 查看全部搜索结果