Interfacial water on collagen nanoribbons by 3D AFM

Collagen is the most abundant structural protein in mammals. Type I collagen in its fibril form has a characteristic pattern structure that alternates two regions called gap and overlap. The structure and properties of collagens are highly dependent on the water and mineral content of the environmen...

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Autores: Arvelo, Diana M., García Sacristán, Clara, Chacón, Enrique, Tarazona Lafarga, Pedro José, García, Ricardo
Tipo de recurso: artículo
Fecha de publicación:2024
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/716439
Acceso en línea:http://hdl.handle.net/10486/716439
https://dx.doi.org/10.1063/5.0205611
Access Level:acceso abierto
Palabra clave:Collagen
structural protein
type I collagen
fibrillar structure
gap and overlap regions
properties of collagen
water and mineral content
3D AFM
structure of interfacial water
Física
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spelling Interfacial water on collagen nanoribbons by 3D AFMArvelo, Diana M.García Sacristán, ClaraChacón, EnriqueTarazona Lafarga, Pedro JoséGarcía, RicardoCollagenstructural proteintype I collagenfibrillar structuregap and overlap regionsproperties of collagenwater and mineral content3D AFMstructure of interfacial waterFísicaCollagen is the most abundant structural protein in mammals. Type I collagen in its fibril form has a characteristic pattern structure that alternates two regions called gap and overlap. The structure and properties of collagens are highly dependent on the water and mineral content of the environment. Here, we apply 3D AFM to characterize at angstrom-scale resolution the interfacial water structure of collagen nanoribbons. For a neutral tip, the interfacial water structure is characterized by the oscillation of the water particle density distribution with a value of 0.3 nm (hydration layers). The interfacial structure does not depend on the collagen region. For a negatively charged tip, the interfacial structure might depend on the collagen region. Hydration layers are observed in overlap regions, while in gap regions, the interfacial solvent structure is dominated by electrostatic interactions. These interactions generate interlayer distances of 0.2 nmWe acknowledge Ministerio de Ciencia e Innovación (Grant No. PID2022-136851NB-I00/AEI/10.13039/501100011033) (R.G.) and the Maria de Maeztu program (Grant No. CEX2018-000805-M).American Institute of Physics Inc.Departamento de Física Teórica de la Materia CondensadaFacultad de Ciencias20242024-04-28research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/716439https://dx.doi.org/10.1063/5.0205611reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/7164392026-06-23T12:46:27Z
dc.title.none.fl_str_mv Interfacial water on collagen nanoribbons by 3D AFM
title Interfacial water on collagen nanoribbons by 3D AFM
spellingShingle Interfacial water on collagen nanoribbons by 3D AFM
Arvelo, Diana M.
Collagen
structural protein
type I collagen
fibrillar structure
gap and overlap regions
properties of collagen
water and mineral content
3D AFM
structure of interfacial water
Física
title_short Interfacial water on collagen nanoribbons by 3D AFM
title_full Interfacial water on collagen nanoribbons by 3D AFM
title_fullStr Interfacial water on collagen nanoribbons by 3D AFM
title_full_unstemmed Interfacial water on collagen nanoribbons by 3D AFM
title_sort Interfacial water on collagen nanoribbons by 3D AFM
dc.creator.none.fl_str_mv Arvelo, Diana M.
García Sacristán, Clara
Chacón, Enrique
Tarazona Lafarga, Pedro José
García, Ricardo
author Arvelo, Diana M.
author_facet Arvelo, Diana M.
García Sacristán, Clara
Chacón, Enrique
Tarazona Lafarga, Pedro José
García, Ricardo
author_role author
author2 García Sacristán, Clara
Chacón, Enrique
Tarazona Lafarga, Pedro José
García, Ricardo
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Física Teórica de la Materia Condensada
Facultad de Ciencias
dc.subject.none.fl_str_mv Collagen
structural protein
type I collagen
fibrillar structure
gap and overlap regions
properties of collagen
water and mineral content
3D AFM
structure of interfacial water
Física
topic Collagen
structural protein
type I collagen
fibrillar structure
gap and overlap regions
properties of collagen
water and mineral content
3D AFM
structure of interfacial water
Física
description Collagen is the most abundant structural protein in mammals. Type I collagen in its fibril form has a characteristic pattern structure that alternates two regions called gap and overlap. The structure and properties of collagens are highly dependent on the water and mineral content of the environment. Here, we apply 3D AFM to characterize at angstrom-scale resolution the interfacial water structure of collagen nanoribbons. For a neutral tip, the interfacial water structure is characterized by the oscillation of the water particle density distribution with a value of 0.3 nm (hydration layers). The interfacial structure does not depend on the collagen region. For a negatively charged tip, the interfacial structure might depend on the collagen region. Hydration layers are observed in overlap regions, while in gap regions, the interfacial solvent structure is dominated by electrostatic interactions. These interactions generate interlayer distances of 0.2 nm
publishDate 2024
dc.date.none.fl_str_mv 2024
2024-04-28
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/716439
https://dx.doi.org/10.1063/5.0205611
url http://hdl.handle.net/10486/716439
https://dx.doi.org/10.1063/5.0205611
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 4.0 International
http://creativecommons.org/licenses/by/4.0/
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 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Institute of Physics Inc.
publisher.none.fl_str_mv American Institute of Physics Inc.
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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