Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations
Recent experiments in function mechanism study reported that a pH low-insertion peptide (pHLIP) can insert into a zwitterionic palmitoyloleoylphosphatidylcholine (POPC) lipid bilayer at acidic pH while binding to the bilayer surface at basic pH. However, the atomic details of the pH-dependent intera...
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sg-ntu-dr.10356-981262023-02-28T17:04:27Z Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations Zhang, Yun Deng, Yonghua Qian, Zhenyu Luo, Yin Mu, Yuguang Wei, Guanghong School of Biological Sciences DRNTU::Science::Biological sciences Recent experiments in function mechanism study reported that a pH low-insertion peptide (pHLIP) can insert into a zwitterionic palmitoyloleoylphosphatidylcholine (POPC) lipid bilayer at acidic pH while binding to the bilayer surface at basic pH. However, the atomic details of the pH-dependent interaction of pHLIP with a POPC bilayer are not well understood. In this study, we investigate the detailed interactions of pHLIP with a POPC bilayer at acidic and basic pH conditions as those used in function mechanism study, using all-atom molecular dynamics (MD) simulations. Simulations have been performed by employing the initial configurations, where pHLIP is placed in aqueous solution, parallel to bilayer surface (system S), partially-inserted (system P), or fully-inserted (system F) in POPC bilayers. On the basis of multiple 200-ns MD simulations, we found (1) pHLIP in system S can spontaneously insert into a POPC bilayer at acidic pH, while binding to the membrane surface at basic pH; (2) pHLIP in system P can insert deep into a POPC bilayer at acidic pH, while it has a tendency to exit, and stays at bilayer surface at basic pH; (3) pHLIP in system F keeps in an α-helical structure at acidic pH while partially unfolding at basic pH. This study provides at atomic-level the pH-induced insertion of pHLIP into POPC bilayer. Published version 2013-07-25T06:32:46Z 2019-12-06T19:50:57Z 2013-07-25T06:32:46Z 2019-12-06T19:50:57Z 2013 2013 Journal Article Deng, Y., Qian, Z., Luo, Y., Zhang, Y., Mu, Y., & Wei, G. (2013). Membrane Binding and Insertion of a pHLIP Peptide Studied by All-Atom Molecular Dynamics Simulations. International Journal of Molecular Sciences, 14(7), 14532-14549. 1422-0067 https://hdl.handle.net/10356/98126 http://hdl.handle.net/10220/12244 10.3390/ijms140714532 23857053 en International journal of molecular sciences © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). application/pdf |
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DRNTU::Science::Biological sciences Zhang, Yun Deng, Yonghua Qian, Zhenyu Luo, Yin Mu, Yuguang Wei, Guanghong Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
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Recent experiments in function mechanism study reported that a pH low-insertion peptide (pHLIP) can insert into a zwitterionic palmitoyloleoylphosphatidylcholine (POPC) lipid bilayer at acidic pH while binding to the bilayer surface at basic pH. However, the atomic details of the pH-dependent interaction of pHLIP with a POPC bilayer are not well understood. In this study, we investigate the detailed interactions of pHLIP with a POPC bilayer at acidic and basic pH conditions as those used in function mechanism study, using all-atom molecular dynamics (MD) simulations. Simulations have been performed by employing the initial configurations, where pHLIP is placed in aqueous solution, parallel to bilayer surface (system S), partially-inserted (system P), or fully-inserted (system F) in POPC bilayers. On the basis of multiple 200-ns MD simulations, we found (1) pHLIP in system S can spontaneously insert into a POPC bilayer at acidic pH, while binding to the membrane surface at basic pH; (2) pHLIP in system P can insert deep into a POPC bilayer at acidic pH, while it has a tendency to exit, and stays at bilayer surface at basic pH; (3) pHLIP in system F keeps in an α-helical structure at acidic pH while partially unfolding at basic pH. This study provides at atomic-level the pH-induced insertion of pHLIP into POPC bilayer. |
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School of Biological Sciences |
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School of Biological Sciences Zhang, Yun Deng, Yonghua Qian, Zhenyu Luo, Yin Mu, Yuguang Wei, Guanghong |
format |
Article |
author |
Zhang, Yun Deng, Yonghua Qian, Zhenyu Luo, Yin Mu, Yuguang Wei, Guanghong |
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Zhang, Yun |
title |
Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
title_short |
Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
title_full |
Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
title_fullStr |
Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
title_full_unstemmed |
Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations |
title_sort |
membrane binding and insertion of a phlip peptide studied by all-atom molecular dynamics simulations |
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2013 |
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https://hdl.handle.net/10356/98126 http://hdl.handle.net/10220/12244 |
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1759854917518884864 |