Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/153448
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dc.contributor.authorChng, Choon-Pengen_US
dc.contributor.authorCho, Nam-Joonen_US
dc.contributor.authorHsia, K. Jimmyen_US
dc.contributor.authorHuang, Changjinen_US
dc.date.accessioned2021-12-03T05:14:42Z-
dc.date.available2021-12-03T05:14:42Z-
dc.date.issued2021-
dc.identifier.citationChng, 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.1c02067en_US
dc.identifier.issn0743-7463en_US
dc.identifier.urihttps://hdl.handle.net/10356/153448-
dc.description.abstractMany 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.en_US
dc.description.sponsorshipMinistry of Education (MOE)en_US
dc.description.sponsorshipNanyang Technological Universityen_US
dc.language.isoenen_US
dc.relationR01HD086325en_US
dc.relationM4082428en_US
dc.relationM4082352en_US
dc.relationRG92/19en_US
dc.relation.ispartofLangmuiren_US
dc.relation.uri10.21979/N9/FPJXJTen_US
dc.rightsThis 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.en_US
dc.subjectScience::Biological sciences::Biophysicsen_US
dc.titleRole of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formationen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Mechanical and Aerospace Engineeringen_US
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.contributor.organizationChina-Singapore International Joint Research Institute (CSIJRI)en_US
dc.identifier.doi10.1021/acs.langmuir.1c02067-
dc.description.versionAccepted versionen_US
dc.identifier.pmid34724382-
dc.identifier.scopus2-s2.0-85119009347-
dc.identifier.issue45en_US
dc.identifier.volume37en_US
dc.identifier.spage13390en_US
dc.identifier.epage13398en_US
dc.subject.keywordsAntiviral Peptideen_US
dc.subject.keywordsMembrane Stretchen_US
dc.description.acknowledgementK.J.H. and C.H. acknowledge the financial support by the National Institutes of Health Eunice Kennedy Shriver National Institute of Child Health and Human Development (Grant R01HD086325). N.-J.C. acknowledges support from the China-Singapore International Joint Research Institute (CSIJRI). K.J.H. acknowledges the financial support by Nanyang Technological University (Start-up Grant M4082428). C.H. also acknowledges the financial support by Nanyang Technological University (Start-up Grant M4082352) and the Ministry of Education, Singapore, under its Academic Research Fund Tier 1 (RG92/19). The computational work for this article was fully performed on resources of the National Supercomputing Centre, Singapore (https://www.nscc.sg).en_US
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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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