In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures

Collagen is the most abundant protein in tissue scaffolds in live organisms. Collagen can self-assemble in vitro, which has led to a number of biotechnological and biomedical applications. To understand the dominant factors that participate in the formation of collagen nanostructures, here we study...

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Autores: García-Sacristán, Clara, Gisbert, Victor G., Klein, Kevin, Šarić, Anđela, García García, Ricardo
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2024
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/383896
Acesso em linha:http://hdl.handle.net/10261/383896
https://api.elsevier.com/content/abstract/scopus_id/85197519642
Access Level:Acceso aberto
Palavra-chave:amino acids
collagen
electrostatic
high-speed AFM
pH
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spelling In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen NanostructuresGarcía-Sacristán, ClaraGisbert, Victor G.Klein, KevinŠarić, AnđelaGarcía García, Ricardoamino acidscollagenelectrostatichigh-speed AFMpHCollagen is the most abundant protein in tissue scaffolds in live organisms. Collagen can self-assemble in vitro, which has led to a number of biotechnological and biomedical applications. To understand the dominant factors that participate in the formation of collagen nanostructures, here we study in real time and with nanoscale resolution the disassembly and reassembly of collagens. We implement a high-speed force microscope, which provides in situ high spatiotemporal resolution images of collagen nanostructures under changing pH conditions. The disassembly and reassembly are dominated by the electrostatic interactions among amino-acid residues of different molecules. Acidic conditions favor disassembly by neutralizing negatively charged residues. The process sets a net repulsive force between collagen molecules. A neutral pH favors the presence of negative and positively charged residues along the collagen molecules, which promotes their electrostatic attraction. Molecular dynamics simulations reproduce the experimental behavior and validate the electrostatic-based model of the disassembly and reassembly processes.We are grateful to Nancy Forde (Simon Fraser University) for her motivating comments. Financial support from the Ministerio de Ciencia, Innovacion y Universidades (PID2019-106801GB-I00 and PID2022-136851NB-I00) is acknowledged. A.S. and K.K. acknowledge support from the Royal Society University Research Fellowship and ERC the European Union's Horizon 2020584 Research and Innovation Programme (Grant No. 585 80296).Supporting InformationPeer reviewedAmerican Chemical Society#NODATA#0000-0002-9164-0411#NODATA#0000-0002-7854-21390000-0002-7115-1928Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/383896https://api.elsevier.com/content/abstract/scopus_id/85197519642reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésACS nanohttps://doi.org/10.1021/acsnano.4c03839Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3838962026-05-22T06:33:51Z
dc.title.none.fl_str_mv In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
title In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
spellingShingle In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
García-Sacristán, Clara
amino acids
collagen
electrostatic
high-speed AFM
pH
title_short In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
title_full In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
title_fullStr In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
title_full_unstemmed In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
title_sort In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures
dc.creator.none.fl_str_mv García-Sacristán, Clara
Gisbert, Victor G.
Klein, Kevin
Šarić, Anđela
García García, Ricardo
author García-Sacristán, Clara
author_facet García-Sacristán, Clara
Gisbert, Victor G.
Klein, Kevin
Šarić, Anđela
García García, Ricardo
author_role author
author2 Gisbert, Victor G.
Klein, Kevin
Šarić, Anđela
García García, Ricardo
author2_role author
author
author
author
dc.contributor.none.fl_str_mv #NODATA#
0000-0002-9164-0411
#NODATA#
0000-0002-7854-2139
0000-0002-7115-1928
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv amino acids
collagen
electrostatic
high-speed AFM
pH
topic amino acids
collagen
electrostatic
high-speed AFM
pH
description Collagen is the most abundant protein in tissue scaffolds in live organisms. Collagen can self-assemble in vitro, which has led to a number of biotechnological and biomedical applications. To understand the dominant factors that participate in the formation of collagen nanostructures, here we study in real time and with nanoscale resolution the disassembly and reassembly of collagens. We implement a high-speed force microscope, which provides in situ high spatiotemporal resolution images of collagen nanostructures under changing pH conditions. The disassembly and reassembly are dominated by the electrostatic interactions among amino-acid residues of different molecules. Acidic conditions favor disassembly by neutralizing negatively charged residues. The process sets a net repulsive force between collagen molecules. A neutral pH favors the presence of negative and positively charged residues along the collagen molecules, which promotes their electrostatic attraction. Molecular dynamics simulations reproduce the experimental behavior and validate the electrostatic-based model of the disassembly and reassembly processes.
publishDate 2024
dc.date.none.fl_str_mv 2024
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/383896
https://api.elsevier.com/content/abstract/scopus_id/85197519642
url http://hdl.handle.net/10261/383896
https://api.elsevier.com/content/abstract/scopus_id/85197519642
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv ACS nano
https://doi.org/10.1021/acsnano.4c03839
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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