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 | Schools: | School of Mechanical and Aerospace Engineering School of Chemical and Biomedical Engineering School of Materials Science and Engineering |
Organisations: | China-Singapore International Joint Research Institute (CSIJRI) | 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: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | MAE Journal Articles MSE Journal Articles SCBE Journal Articles |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Langmuir_AH_peptide_manuscript_accepted.pdf | Manuscript | 1.79 MB | Adobe PDF | View/Open |
Langmuir_AH_peptide_Supporting_Information_accepted.pdf | Supporting Information | 597.4 kB | Adobe PDF | View/Open |
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