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Journal of Genetics and DNA Research

ISSN: 2684-6039

Open Access

Role of aromatic interaction in adhesion of amyloid beta peptides on glycolipid containing membrane

Abstract

Vahed Majid

The CH−π and OH−π interaction of aromatic residues of amyloid beta (Aβ) with GM1 oligosaccharide is concluded to be effective to keep Aβ peptides attached to the membrane surface and play an important role to initial stages of Alzheimer’s disease pathology. In this work, molecular dynamics (MD) simulations for Aβ42 were performed to investigate the behaviors of Aβ42 on GM1- ganglioside-containing lipid membrane. As far the computational model, the initial atom coordinate of Aβ42 were extracted from one of the conformations which had been determined by solution nuclear magnetic resonance (NMR) spectroscopy (PDB accession code: 1Z0Q/1IYT). A computational model for mixed membrane was composed of 48 monosialotetrahexosylganglioside (GM1), 96 sphingomyelin (SM), and 96 cholesterol(CHL).

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