Assessing the interaction between surfactant-like peptides and lipid membranes
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/55508 http://dx.doi.org/10.1039/c7ra04537a |
Resumo: | Atomistic molecular dynamics simulations were used to study the interaction of AnK peptides (with n = 3, 6 and 9) in contact with two different types of lipid membranes, DPPC and DPPG. PMF calculations and their decomposition into enthalpic and entropic components allowed a detailed thermodynamic analysis of the energy profile associated with the adsorption and penetration of the peptides through the lipid membranes. Our simulations indicated a drastic difference between the interactions of the peptides with both membranes. For the peptide A6K the interaction with the DPPG and DPPC membranes were -222 kJ mol(-1) and-16 kJ mol(-1), respectively. PMF for the DPPC membrane did not show any minimum in the interface region, that is, no favorable interaction with its surface. On the other hand, the interaction with the DPPG membrane showed a clear minimum near the surface. This minimum, although shallow, -10 kJ mol(-1,) indicates that the adhesion of the AnK peptides on the surface of the DPPG membranes is a favorable process. |
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Malaspina, Thaciana [UNIFESP]Colherinhas, GuilhermeOuti, Felipe de Oliveira [UNIFESP]Fileti, Eudes E. [UNIFESP]2020-07-17T14:03:34Z2020-07-17T14:03:34Z2017Rsc Advances. Cambridge, v. 7, n. 57, p. 35973-35981, 2017.2046-2069https://repositorio.unifesp.br/handle/11600/55508http://dx.doi.org/10.1039/c7ra04537aWOS000406104300049.pdf10.1039/c7ra04537aWOS:000406104300049Atomistic molecular dynamics simulations were used to study the interaction of AnK peptides (with n = 3, 6 and 9) in contact with two different types of lipid membranes, DPPC and DPPG. PMF calculations and their decomposition into enthalpic and entropic components allowed a detailed thermodynamic analysis of the energy profile associated with the adsorption and penetration of the peptides through the lipid membranes. Our simulations indicated a drastic difference between the interactions of the peptides with both membranes. For the peptide A6K the interaction with the DPPG and DPPC membranes were -222 kJ mol(-1) and-16 kJ mol(-1), respectively. PMF for the DPPC membrane did not show any minimum in the interface region, that is, no favorable interaction with its surface. On the other hand, the interaction with the DPPG membrane showed a clear minimum near the surface. This minimum, although shallow, -10 kJ mol(-1,) indicates that the adhesion of the AnK peptides on the surface of the DPPG membranes is a favorable process.CAPESFAPESPFAPEGUniv Fed Goias, CEPAE, Dept Fis, CP 131, BR-74001970 Goiania, Go, BrazilUniv Fed Sao Paulo, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, BrazilUniv Fed Sao Paulo, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, SP, BrazilWeb of Science35973-35981engRoyal Soc ChemistryRsc AdvancesAssessing the interaction between surfactant-like peptides and lipid membranesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleCambridge757info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000406104300049.pdfapplication/pdf1029880${dspace.ui.url}/bitstream/11600/55508/1/WOS000406104300049.pdf94499f1aa90266d2c42cf63e77858cd3MD51open accessTEXTWOS000406104300049.pdf.txtWOS000406104300049.pdf.txtExtracted texttext/plain36658${dspace.ui.url}/bitstream/11600/55508/8/WOS000406104300049.pdf.txt775ae9105b3da79f864574d67fd0eed7MD58open accessTHUMBNAILWOS000406104300049.pdf.jpgWOS000406104300049.pdf.jpgIM Thumbnailimage/jpeg7473${dspace.ui.url}/bitstream/11600/55508/10/WOS000406104300049.pdf.jpg2eb899c0de39acd35f84a02cf8a79db3MD510open access11600/555082023-06-05 19:07:34.821open accessoai:repositorio.unifesp.br:11600/55508Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-06-05T22:07:34Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Assessing the interaction between surfactant-like peptides and lipid membranes |
title |
Assessing the interaction between surfactant-like peptides and lipid membranes |
spellingShingle |
Assessing the interaction between surfactant-like peptides and lipid membranes Malaspina, Thaciana [UNIFESP] |
title_short |
Assessing the interaction between surfactant-like peptides and lipid membranes |
title_full |
Assessing the interaction between surfactant-like peptides and lipid membranes |
title_fullStr |
Assessing the interaction between surfactant-like peptides and lipid membranes |
title_full_unstemmed |
Assessing the interaction between surfactant-like peptides and lipid membranes |
title_sort |
Assessing the interaction between surfactant-like peptides and lipid membranes |
author |
Malaspina, Thaciana [UNIFESP] |
author_facet |
Malaspina, Thaciana [UNIFESP] Colherinhas, Guilherme Outi, Felipe de Oliveira [UNIFESP] Fileti, Eudes E. [UNIFESP] |
author_role |
author |
author2 |
Colherinhas, Guilherme Outi, Felipe de Oliveira [UNIFESP] Fileti, Eudes E. [UNIFESP] |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Malaspina, Thaciana [UNIFESP] Colherinhas, Guilherme Outi, Felipe de Oliveira [UNIFESP] Fileti, Eudes E. [UNIFESP] |
description |
Atomistic molecular dynamics simulations were used to study the interaction of AnK peptides (with n = 3, 6 and 9) in contact with two different types of lipid membranes, DPPC and DPPG. PMF calculations and their decomposition into enthalpic and entropic components allowed a detailed thermodynamic analysis of the energy profile associated with the adsorption and penetration of the peptides through the lipid membranes. Our simulations indicated a drastic difference between the interactions of the peptides with both membranes. For the peptide A6K the interaction with the DPPG and DPPC membranes were -222 kJ mol(-1) and-16 kJ mol(-1), respectively. PMF for the DPPC membrane did not show any minimum in the interface region, that is, no favorable interaction with its surface. On the other hand, the interaction with the DPPG membrane showed a clear minimum near the surface. This minimum, although shallow, -10 kJ mol(-1,) indicates that the adhesion of the AnK peptides on the surface of the DPPG membranes is a favorable process. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2020-07-17T14:03:34Z |
dc.date.available.fl_str_mv |
2020-07-17T14:03:34Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Rsc Advances. Cambridge, v. 7, n. 57, p. 35973-35981, 2017. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/55508 http://dx.doi.org/10.1039/c7ra04537a |
dc.identifier.issn.none.fl_str_mv |
2046-2069 |
dc.identifier.file.none.fl_str_mv |
WOS000406104300049.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1039/c7ra04537a |
dc.identifier.wos.none.fl_str_mv |
WOS:000406104300049 |
identifier_str_mv |
Rsc Advances. Cambridge, v. 7, n. 57, p. 35973-35981, 2017. 2046-2069 WOS000406104300049.pdf 10.1039/c7ra04537a WOS:000406104300049 |
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https://repositorio.unifesp.br/handle/11600/55508 http://dx.doi.org/10.1039/c7ra04537a |
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eng |
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eng |
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Rsc Advances |
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35973-35981 |
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Cambridge |
dc.publisher.none.fl_str_mv |
Royal Soc Chemistry |
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Royal Soc Chemistry |
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