Thermomechanical response of a representative porin for biomimetics

The thermomechanical response of Omp2a, a representative porin used for the fabrication of smart biomimetic nanomembranes, has been characterized using microcantilever technology and compared with standard proteins. For this purpose, thermally induced transitions involving the conversion of stable t...

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Autores: Lopes Rodrigues, Maximilien|||0000-0002-9405-336X, Puiggalí Jou, Anna|||0000-0002-2234-9436, Martí Ballesté, Didac, Valle Mendoza, Luis Javier del|||0000-0001-9916-1741, Michaux, Catherine Anne Gisèle, Perpète, Eric A., Alemán Llansó, Carlos|||0000-0003-4462-6075
Tipo de recurso: artículo
Fecha de publicación:2018
País:España
Institución:Universitat Politècnica de Catalunya (UPC)
Repositorio:UPCommons. Portal del coneixement obert de la UPC
Idioma:inglés
OAI Identifier:oai:upcommons.upc.edu:2117/130343
Acceso en línea:https://hdl.handle.net/2117/130343
https://dx.doi.org/10.1021/acsomega.8b00463
Access Level:acceso abierto
Palabra clave:Proteins
Molecular dynamics
Albumins
Mechanical properties
Thermal properties
Proteïnes
Dinàmica molecular
Àrees temàtiques de la UPC::Enginyeria química
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spelling Thermomechanical response of a representative porin for biomimeticsLopes Rodrigues, Maximilien|||0000-0002-9405-336XPuiggalí Jou, Anna|||0000-0002-2234-9436Martí Ballesté, DidacValle Mendoza, Luis Javier del|||0000-0001-9916-1741Michaux, Catherine Anne GisèlePerpète, Eric A.Alemán Llansó, Carlos|||0000-0003-4462-6075ProteinsMolecular dynamicsAlbuminsMechanical propertiesMolecular dynamicsProteinsThermal propertiesProteïnesDinàmica molecularÀrees temàtiques de la UPC::Enginyeria químicaThe thermomechanical response of Omp2a, a representative porin used for the fabrication of smart biomimetic nanomembranes, has been characterized using microcantilever technology and compared with standard proteins. For this purpose, thermally induced transitions involving the conversion of stable trimers to bigger aggregates, local reorganizations based on the strengthening or weakening of intermolecular interactions, and protein denaturation have been detected by the microcantilever resonance frequency and deflection as a function of the temperature. Measurements have been carried out on arrays of 8-microcantilevers functionalized with proteins (Omp2a, lysozyme and bovine serum albumin). To interpret the measured nanofeatures, the response of proteins to temperature has been also examined using other characterization techniques, including real time wide angle X-ray diffraction. Results not only demonstrate the complex behavior of porins, which exhibit multiple local thermal transitions before undergoing denaturation at temperatures higher than 105 °C, but also suggest a posttreatment to control the orientation of immobilized Omp2a molecules in functionalized biomimetic nanomembranes and, thus, increase their efficacy in ion transport.Peer ReviewedAmerican Chemical Society (ACS)20182018-07-3120192019-03-13journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/2117/130343https://dx.doi.org/10.1021/acsomega.8b00463reponame:UPCommons. Portal del coneixement obert de la UPCinstname:Universitat Politècnica de Catalunya (UPC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivs 3.0 Spainhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/info:eu-repo/semantics/openAccessoai:upcommons.upc.edu:2117/1303432026-05-27T15:37:01Z
dc.title.none.fl_str_mv Thermomechanical response of a representative porin for biomimetics
title Thermomechanical response of a representative porin for biomimetics
spellingShingle Thermomechanical response of a representative porin for biomimetics
Lopes Rodrigues, Maximilien|||0000-0002-9405-336X
Proteins
Molecular dynamics
Albumins
Mechanical properties
Molecular dynamics
Proteins
Thermal properties
Proteïnes
Dinàmica molecular
Àrees temàtiques de la UPC::Enginyeria química
title_short Thermomechanical response of a representative porin for biomimetics
title_full Thermomechanical response of a representative porin for biomimetics
title_fullStr Thermomechanical response of a representative porin for biomimetics
title_full_unstemmed Thermomechanical response of a representative porin for biomimetics
title_sort Thermomechanical response of a representative porin for biomimetics
dc.creator.none.fl_str_mv Lopes Rodrigues, Maximilien|||0000-0002-9405-336X
Puiggalí Jou, Anna|||0000-0002-2234-9436
Martí Ballesté, Didac
Valle Mendoza, Luis Javier del|||0000-0001-9916-1741
Michaux, Catherine Anne Gisèle
Perpète, Eric A.
Alemán Llansó, Carlos|||0000-0003-4462-6075
author Lopes Rodrigues, Maximilien|||0000-0002-9405-336X
author_facet Lopes Rodrigues, Maximilien|||0000-0002-9405-336X
Puiggalí Jou, Anna|||0000-0002-2234-9436
Martí Ballesté, Didac
Valle Mendoza, Luis Javier del|||0000-0001-9916-1741
Michaux, Catherine Anne Gisèle
Perpète, Eric A.
Alemán Llansó, Carlos|||0000-0003-4462-6075
author_role author
author2 Puiggalí Jou, Anna|||0000-0002-2234-9436
Martí Ballesté, Didac
Valle Mendoza, Luis Javier del|||0000-0001-9916-1741
Michaux, Catherine Anne Gisèle
Perpète, Eric A.
Alemán Llansó, Carlos|||0000-0003-4462-6075
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteins
Molecular dynamics
Albumins
Mechanical properties
Molecular dynamics
Proteins
Thermal properties
Proteïnes
Dinàmica molecular
Àrees temàtiques de la UPC::Enginyeria química
topic Proteins
Molecular dynamics
Albumins
Mechanical properties
Molecular dynamics
Proteins
Thermal properties
Proteïnes
Dinàmica molecular
Àrees temàtiques de la UPC::Enginyeria química
description The thermomechanical response of Omp2a, a representative porin used for the fabrication of smart biomimetic nanomembranes, has been characterized using microcantilever technology and compared with standard proteins. For this purpose, thermally induced transitions involving the conversion of stable trimers to bigger aggregates, local reorganizations based on the strengthening or weakening of intermolecular interactions, and protein denaturation have been detected by the microcantilever resonance frequency and deflection as a function of the temperature. Measurements have been carried out on arrays of 8-microcantilevers functionalized with proteins (Omp2a, lysozyme and bovine serum albumin). To interpret the measured nanofeatures, the response of proteins to temperature has been also examined using other characterization techniques, including real time wide angle X-ray diffraction. Results not only demonstrate the complex behavior of porins, which exhibit multiple local thermal transitions before undergoing denaturation at temperatures higher than 105 °C, but also suggest a posttreatment to control the orientation of immobilized Omp2a molecules in functionalized biomimetic nanomembranes and, thus, increase their efficacy in ion transport.
publishDate 2018
dc.date.none.fl_str_mv 2018
2018-07-31
2019
2019-03-13
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/2117/130343
https://dx.doi.org/10.1021/acsomega.8b00463
url https://hdl.handle.net/2117/130343
https://dx.doi.org/10.1021/acsomega.8b00463
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivs 3.0 Spain
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivs 3.0 Spain
http://creativecommons.org/licenses/by-nc-nd/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Chemical Society (ACS)
publisher.none.fl_str_mv American Chemical Society (ACS)
dc.source.none.fl_str_mv reponame:UPCommons. Portal del coneixement obert de la UPC
instname:Universitat Politècnica de Catalunya (UPC)
instname_str Universitat Politècnica de Catalunya (UPC)
reponame_str UPCommons. Portal del coneixement obert de la UPC
collection UPCommons. Portal del coneixement obert de la UPC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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