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Plos One : Binding, Conformational Transition and Dimerization of Amyloid-β Peptide on Gm1-containing Ternary Membrane ; Insights from Molecular Dynamics Simulation, Volume 8

By Zheng, Jie

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Book Id: WPLBN0003944570
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Reproduction Date: 2015

Title: Plos One : Binding, Conformational Transition and Dimerization of Amyloid-β Peptide on Gm1-containing Ternary Membrane ; Insights from Molecular Dynamics Simulation, Volume 8  
Author: Zheng, Jie
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
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Publisher: Plos

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Zheng, J. (n.d.). Plos One : Binding, Conformational Transition and Dimerization of Amyloid-β Peptide on Gm1-containing Ternary Membrane ; Insights from Molecular Dynamics Simulation, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : Interactions of amyloid-b (Ab) with neuronal membrane are associated with the progression of Alzheimer’s disease (AD). Ganglioside GM1 has been shown to promote the structural conversion of Ab and increase the rate of peptide aggregation: but the exact nature of interaction driving theses processes remains to be explored. In this work, we have carried out atomistic-scale computer simulations (totaling 2.65 ms) to investigate the behavior of Ab monomer and dimers in GM1- containing raft-like membrane. The oligosaccharide head-group of GM1 was observed to act as scaffold for Ab-binding through sugar-specific interactions. Starting from the initial helical peptide conformation, a b-hairpin motif was formed at the C-terminus of the GM1-bound Ab-monomer: that didn’t appear in absence of GM1 (both in fluid POPC and liquidordered cholesterol/POPC bilayers and also in aqueous medium) within the simulation time span. For Ab-dimers, the bstructure was further enhanced by peptide-peptide interactions, which might influence the propensity of Ab to aggregate into higher-ordered structures. The salt-bridges and inter-peptide hydrogen bonds were found to account for dimer stability. We observed spontaneous formation of intra-peptide D23-K28 salt-bridge and a turn at V24GSN27 region - long been accepted as characteristic structural-motifs for amyloid self-assembly. Altogether, our results provide atomistic details of Ab- GM1 and Ab-Ab interactions and demonstrate their importance in the early-stages of GM1-mediated Ab-oligomerisation on membrane surface

 

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