Molecular dynamics study on the effects of charged amino acid distribution under low pH condition to the unfolding of hen egg white lysozyme and formation of beta strands

บทความในวารสาร

ผู้เขียน/บรรณาธิการ

กลุ่มสาขาการวิจัยเชิงกลยุทธ์

รายละเอียดสำหรับงานพิมพ์

รายชื่อผู้แต่ง: Zein, Husnul Fuad; Alam, Ibrar; Asanithi, Piyapong; Sutthibutpong, Thana;

ผู้เผยแพร่: Public Library of Science

ปีที่เผยแพร่ (ค.ศ.): 2022

วารสาร: PLoS ONE (1932-6203)

Volume number: 17

Issue number: 3

นอก: 1932-6203

eISSN: 1932-6203

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85126976803&doi=10.1371%2fjournal.pone.0249742&partnerID=40&md5=523edcb494534cda55da5586e2354ad0

ภาษา: English-Great Britain (EN-GB)

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บทคัดย่อ

Aggregation of unfolded or misfolded proteins into amyloid fibrils can cause various diseases in humans. However, the fibrils synthesized in vitro can be developed toward useful biomaterials under some physicochemical conditions. In this study, atomistic molecular dynamics simulations were performed to address the mechanism of beta-sheet formation of the unfolded hen egg-white lysozyme (HEWL) under a high temperature and low pH. Simulations of the protonated HEWL at pH 2 and the non-protonated HEWL at pH 7 were performed at the highly elevated temperature of 450 K to accelerate the unfolding, followed by the 333 K temperature to emulate some previous in vitro studies. The simulations showed that HEWL unfolded faster, and higher beta-strand contents were observed at pH 2. In addition, one of the simulation replicas at pH 2 showed that the beta-strand forming sequence was consistent with the 'K-peptide', proposed as the core region for amyloidosis in previous experimental studies. Beta-strand formation mechanisms at the earlier stage of amyloidosis were explained in terms of the radial distribution of the amino acids. The separation between groups of positively charged sidechains from the hydrophobic core corresponded to the clustering of the hydrophobic residues and beta-strand formation. © 2022 Zein et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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