How procyanidin C1 sticks to collagen : the role of proline rings

Autores
Petelski, Andre Nicolai; Pamies, Silvana Carina; Sosa, Gladis Laura
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between –OH groups of the polyphenol and C––O groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is C–H⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.
Fil: Petelski, Andre Nicolai. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Petelski, André Nicolai. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.
Fil: Pamies, Silvana Carina. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina.
Fil: Sosa, Gladis Laura. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Sosa, Gladis Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.
Peer Reviewed
Materia
Hydrogen bonds
Stacking
Proline
Polyphenol
Protein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
2023-10-27T22:08:44Z
Repositorio
Repositorio Institucional Abierto (UTN)
Institución
Universidad Tecnológica Nacional
OAI Identificador
oai:ria.utn.edu.ar:20.500.12272/8651
Acceder
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oai_identifier_str oai:ria.utn.edu.ar:20.500.12272/8651
network_acronym_str RIAUTN
repository_id_str a
network_name_str Repositorio Institucional Abierto (UTN)
spelling How procyanidin C1 sticks to collagen : the role of proline ringsPetelski, Andre NicolaiPamies, Silvana CarinaSosa, Gladis LauraHydrogen bondsStackingProlinePolyphenolProteinMolecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between –OH groups of the polyphenol and C––O groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is C–H⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.Fil: Petelski, Andre Nicolai. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Petelski, André Nicolai. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.Fil: Pamies, Silvana Carina. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina.Fil: Sosa, Gladis Laura. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Sosa, Gladis Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.Peer Reviewed2023-10-27T22:08:44Z2023-10-27T22:08:44Z2021-05-29info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articulopdfapplication/pdfhttp://hdl.handle.net/20.500.12272/8651https://doi.org/10.1016/j.bpc.2021.106627enginfo:eu-repo/semantics/openAccess2023-10-27T22:08:44ZAcceso abiertoreponame:Repositorio Institucional Abierto (UTN)instname:Universidad Tecnológica Nacional2026-09-24T12:46:33Zoai:ria.utn.edu.ar:20.500.12272/8651instacron:UTNInstitucionalhttp://ria.utn.edu.ar/Universidad públicaNo correspondehttp://ria.utn.edu.ar/oaigestionria@rec.utn.edu.ar; fsuarez@rec.utn.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2026-09-24 12:46:34.123Repositorio Institucional Abierto (UTN) - Universidad Tecnológica Nacionalfalse
dc.title.none.fl_str_mv How procyanidin C1 sticks to collagen : the role of proline rings
title How procyanidin C1 sticks to collagen : the role of proline rings
spellingShingle How procyanidin C1 sticks to collagen : the role of proline rings
Petelski, Andre Nicolai
Hydrogen bonds
Stacking
Proline
Polyphenol
Protein
title_short How procyanidin C1 sticks to collagen : the role of proline rings
title_full How procyanidin C1 sticks to collagen : the role of proline rings
title_fullStr How procyanidin C1 sticks to collagen : the role of proline rings
title_full_unstemmed How procyanidin C1 sticks to collagen : the role of proline rings
title_sort How procyanidin C1 sticks to collagen : the role of proline rings
dc.creator.none.fl_str_mv Petelski, Andre Nicolai
Pamies, Silvana Carina
Sosa, Gladis Laura
author Petelski, Andre Nicolai
author_facet Petelski, Andre Nicolai
Pamies, Silvana Carina
Sosa, Gladis Laura
author_role author
author2 Pamies, Silvana Carina
Sosa, Gladis Laura
author2_role author
author
dc.subject.none.fl_str_mv Hydrogen bonds
Stacking
Proline
Polyphenol
Protein
topic Hydrogen bonds
Stacking
Proline
Polyphenol
Protein
dc.description.none.fl_txt_mv Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between –OH groups of the polyphenol and C––O groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is C–H⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.
Fil: Petelski, Andre Nicolai. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Petelski, André Nicolai. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.
Fil: Pamies, Silvana Carina. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina.
Fil: Sosa, Gladis Laura. Universidad Tecnológica Nacional. Facultad Regional Resistencia. Grupo de Investigación Química Teórica Experimental; Argentina. Fil: Sosa, Gladis Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina.
Peer Reviewed
description Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between –OH groups of the polyphenol and C––O groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is C–H⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.
publishDate 2021
dc.date.none.fl_str_mv 2021-05-29
2023-10-27T22:08:44Z
2023-10-27T22:08:44Z
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12272/8651
https://doi.org/10.1016/j.bpc.2021.106627
url http://hdl.handle.net/20.500.12272/8651
https://doi.org/10.1016/j.bpc.2021.106627
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
2023-10-27T22:08:44Z
Acceso abierto
eu_rights_str_mv openAccess
rights_invalid_str_mv 2023-10-27T22:08:44Z
Acceso abierto
dc.format.none.fl_str_mv pdf
application/pdf
dc.source.none.fl_str_mv reponame:Repositorio Institucional Abierto (UTN)
instname:Universidad Tecnológica Nacional
reponame_str Repositorio Institucional Abierto (UTN)
collection Repositorio Institucional Abierto (UTN)
instname_str Universidad Tecnológica Nacional
repository.name.fl_str_mv Repositorio Institucional Abierto (UTN) - Universidad Tecnológica Nacional
repository.mail.fl_str_mv gestionria@rec.utn.edu.ar; fsuarez@rec.utn.edu.ar
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score 13.265058

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