Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/xmlui/handle/123456789/19739
Title: Mechanism of Initiation, Association, and Formation of Amyloid Fibrils Modeled with the N-Terminal Peptide Fragment, IKYLEFIS, of Myoglobin G-Helix
Authors: PATEL, S
SASIDHAR, YU
CHARY, KVR
Keywords: Particle Mesh Ewald
Protein Aggregation
Beta-Peptide
Atomistic Simulations
Computer-Simulations
Oligomer Formation
Human Lysozyme
Force-Field
Stability
Disease
Issue Date: 2017
Publisher: AMER CHEMICAL SOC
Citation: JOURNAL OF PHYSICAL CHEMISTRY B,121(32)7536-7549
Abstract: Some peptides and proteins undergo self-aggregation under certain conditions, leading to amyloid fibrils formation, which is related to many disease conditions. It is important to understand such amyloid fibrils formation to provide mechanistic detail that governs the process. A predominantly alpha-helical myoglobin has been reported recently to readily form amyloid fibrils at a higher temperature, similar to its G-helix segment. Here, we have investigated the mechanism of amyloid fibrils formation by performing multiple long molecular dynamics simulations (27 mu s) on the N-terminal segment of the G-helix of myoglobin. These simulations resulted in the formation of a single-layered tetrameric beta-sheet with mixed parallel and antiparallel beta-strands and this is the most common event irrespective of many different starting structures. Formation of the single-layered tetrameric beta-sheet takes place following three distinctive pathways. The process of fibril initiation is dependent on temperature. Further, this study provides mechanistic insights into the formation of multilayered fibrilar structure, which could be applicable to a wider variety of peptides or proteins to understand the amyloidogenesis.
URI: http://dx.doi.org/10.1021/acs.jpcb.7b02205
http://localhost:8080/xmlui/handle/123456789/19739
ISSN: 1520-6106
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