Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/153448
Title: Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation
Authors: Chng, Choon-Peng
Cho, Nam-Joon
Hsia, K. Jimmy
Huang, Changjin
Keywords: Science::Biological sciences::Biophysics
Issue Date: 2021
Source: Chng, C., Cho, N., Hsia, K. J. & Huang, C. (2021). Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation. Langmuir, 37(45), 13390-13398. https://dx.doi.org/10.1021/acs.langmuir.1c02067
Project: R01HD086325
M4082428
M4082352
RG92/19
Journal: Langmuir 
Abstract: Many medically important viruses are enveloped viruses, which are surrounded by a structurally conserved, host-derived lipid membrane coating. Agents that target and disrupt this membrane coating could potentially function as broad-spectrum antiviral drugs. The amphipathic α-helical (AH) peptide derived from the N-terminus of the hepatitis C virus NS5A protein is one such candidate and has been demonstrated to be able to selectively rupture lipid vesicles in the size range of viruses (<160 nm diameter). However, the mechanism underlying this membrane curvature selectivity remains elusive. In this study, we have performed molecular dynamics simulations to study the binding of the AH peptide to model membranes that are stretched to resemble the looser lipid headgroup packing present on highly curved outer membranes of nanoscale vesicles. We found that the AH peptide binds more favorably to membranes that are stretched. In addition, a tetrameric placement of peptides across the membrane induced stable pore formation in the stretched membrane. Thus, our results suggest that the AH peptide senses the high curvature of nanoscale vesicles via the enhanced exposure of lipid packing defects induced by membrane area strain.
URI: https://hdl.handle.net/10356/153448
ISSN: 0743-7463
DOI: 10.1021/acs.langmuir.1c02067
DOI (Related Dataset): 10.21979/N9/FPJXJT
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.langmuir.1c02067.
Fulltext Permission: embargo_20221123
Fulltext Availability: With Fulltext
Appears in Collections:MAE Journal Articles
MSE Journal Articles
SCBE Journal Articles

Files in This Item:
File Description SizeFormat 
Langmuir_AH_peptide_manuscript_accepted.pdf
  Until 2022-11-23
Manuscript1.79 MBAdobe PDFUnder embargo until Nov 23, 2022
Langmuir_AH_peptide_Supporting_Information_accepted.pdf
  Until 2022-11-23
Supporting Information597.4 kBAdobe PDFUnder embargo until Nov 23, 2022

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