Water-driven stabilization of diphenylalanine nanotube structures
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s00214-016-1936-3 http://hdl.handle.net/11449/173253 |
Resumo: | L,L-diphenylalanine has been employed in the formation of self-assembled peptide nanotubes with great potential for the development of biosensors, molecular carriers, and optoelectronic devices. They are usually formed in an aqueous solution, and it is well known that water remains confined inside the structure. However, the role played by water in the overall stability of the nanotube is still unknown at the microscopic level. In this work, we investigate the stability of peptide structures after assembly due to the interaction with water molecules. We demonstrate, using molecular dynamics based on density functional tight-binding techniques, that water is fundamental in keeping the nanotube structure. It interacts with the nanotube walls as well as with other water molecules via hydrogen bonds keeping the structure stable. We identify and quantify the interaction between water and the relevant groups, and, upon increasing the solvent concentration, we show there is a transition region where there is a competition between the formation of water/water hydrogen bonds, and steric effects. |
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Water-driven stabilization of diphenylalanine nanotube structuresDFTBPeptide nanotubesStructural stabilityWater propertiesL,L-diphenylalanine has been employed in the formation of self-assembled peptide nanotubes with great potential for the development of biosensors, molecular carriers, and optoelectronic devices. They are usually formed in an aqueous solution, and it is well known that water remains confined inside the structure. However, the role played by water in the overall stability of the nanotube is still unknown at the microscopic level. In this work, we investigate the stability of peptide structures after assembly due to the interaction with water molecules. We demonstrate, using molecular dynamics based on density functional tight-binding techniques, that water is fundamental in keeping the nanotube structure. It interacts with the nanotube walls as well as with other water molecules via hydrogen bonds keeping the structure stable. We identify and quantify the interaction between water and the relevant groups, and, upon increasing the solvent concentration, we show there is a transition region where there is a competition between the formation of water/water hydrogen bonds, and steric effects.Faculdade de Física Universidade Federal do Sul e Sudeste do Pará (UNIFESSPA)Centro de Ciências Naturais e Humanas Universidade Federal do ABCInstituto de Física Teórica Universidade Estadual Paulista (UNESP)Instituto de Física Teórica Universidade Estadual Paulista (UNESP)Universidade Federal do Sul e Sudeste do Pará (UNIFESSPA)Universidade Federal do ABC (UFABC)Universidade Estadual Paulista (Unesp)Andrade-Filho, T.Martins, Tiago CarvalhoFerreira, Fabio FurlanAlves, Wendel AndradeRocha, Alexandre Reily [UNESP]2018-12-11T17:04:21Z2018-12-11T17:04:21Z2016-08-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1007/s00214-016-1936-3Theoretical Chemistry Accounts, v. 135, n. 8, 2016.1432-881Xhttp://hdl.handle.net/11449/17325310.1007/s00214-016-1936-32-s2.0-849788239262-s2.0-84978823926.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengTheoretical Chemistry Accountsinfo:eu-repo/semantics/openAccess2023-11-12T06:13:29Zoai:repositorio.unesp.br:11449/173253Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:29:15.494023Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Water-driven stabilization of diphenylalanine nanotube structures |
title |
Water-driven stabilization of diphenylalanine nanotube structures |
spellingShingle |
Water-driven stabilization of diphenylalanine nanotube structures Andrade-Filho, T. DFTB Peptide nanotubes Structural stability Water properties |
title_short |
Water-driven stabilization of diphenylalanine nanotube structures |
title_full |
Water-driven stabilization of diphenylalanine nanotube structures |
title_fullStr |
Water-driven stabilization of diphenylalanine nanotube structures |
title_full_unstemmed |
Water-driven stabilization of diphenylalanine nanotube structures |
title_sort |
Water-driven stabilization of diphenylalanine nanotube structures |
author |
Andrade-Filho, T. |
author_facet |
Andrade-Filho, T. Martins, Tiago Carvalho Ferreira, Fabio Furlan Alves, Wendel Andrade Rocha, Alexandre Reily [UNESP] |
author_role |
author |
author2 |
Martins, Tiago Carvalho Ferreira, Fabio Furlan Alves, Wendel Andrade Rocha, Alexandre Reily [UNESP] |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal do Sul e Sudeste do Pará (UNIFESSPA) Universidade Federal do ABC (UFABC) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Andrade-Filho, T. Martins, Tiago Carvalho Ferreira, Fabio Furlan Alves, Wendel Andrade Rocha, Alexandre Reily [UNESP] |
dc.subject.por.fl_str_mv |
DFTB Peptide nanotubes Structural stability Water properties |
topic |
DFTB Peptide nanotubes Structural stability Water properties |
description |
L,L-diphenylalanine has been employed in the formation of self-assembled peptide nanotubes with great potential for the development of biosensors, molecular carriers, and optoelectronic devices. They are usually formed in an aqueous solution, and it is well known that water remains confined inside the structure. However, the role played by water in the overall stability of the nanotube is still unknown at the microscopic level. In this work, we investigate the stability of peptide structures after assembly due to the interaction with water molecules. We demonstrate, using molecular dynamics based on density functional tight-binding techniques, that water is fundamental in keeping the nanotube structure. It interacts with the nanotube walls as well as with other water molecules via hydrogen bonds keeping the structure stable. We identify and quantify the interaction between water and the relevant groups, and, upon increasing the solvent concentration, we show there is a transition region where there is a competition between the formation of water/water hydrogen bonds, and steric effects. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-08-01 2018-12-11T17:04:21Z 2018-12-11T17:04:21Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s00214-016-1936-3 Theoretical Chemistry Accounts, v. 135, n. 8, 2016. 1432-881X http://hdl.handle.net/11449/173253 10.1007/s00214-016-1936-3 2-s2.0-84978823926 2-s2.0-84978823926.pdf |
url |
http://dx.doi.org/10.1007/s00214-016-1936-3 http://hdl.handle.net/11449/173253 |
identifier_str_mv |
Theoretical Chemistry Accounts, v. 135, n. 8, 2016. 1432-881X 10.1007/s00214-016-1936-3 2-s2.0-84978823926 2-s2.0-84978823926.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Theoretical Chemistry Accounts |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128817534861312 |