Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation

Autores
Torres, Paola Beatriz; Bojanich, Luciano; Sanchez Varretti, Fabricio Orlando; Ramirez Pastor, Antonio Jose; Quiroga, Evelina; Boeris, Valeria; Narambuena, Claudio Fabian
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this work, the molecular interaction between the protein β-lactoglobulin and strong polyelectrolyte chains was studied using Monte Carlo simulations. Different coarse-grained models were used to represent the system components. Both net charge and protonation of the isolated dimeric protein were analyzed as a function of pH. The acid-base equilibrium of each titratable group was distinctively modified by the presence of polyanion or polycation chains. The complexation on the wrong side of pI was more evident with the polycation than with the polyanion. It was mainly due to a charge regulation mechanism, where the reversion in net charge of the protein was more pronounced at the left of isoelectric point of the protein. The glutamic and aspartic groups play a key role in this charge reversion. Both polyanion and polycation were spatially adsorbed in different region on the protein surface, suggesting the importance of the surface charge distribution of the protein.
Fil: Torres, Paola Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
Fil: Bojanich, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Sanchez Varretti, Fabricio Orlando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
Fil: Ramirez Pastor, Antonio Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina
Fil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina
Fil: Narambuena, Claudio Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
Materia
Whey proteins
Polyelectrolyte
β-lactoglobulin
Complex
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/44507
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/44507
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulationTorres, Paola BeatrizBojanich, LucianoSanchez Varretti, Fabricio OrlandoRamirez Pastor, Antonio JoseQuiroga, EvelinaBoeris, ValeriaNarambuena, Claudio FabianWhey proteinsPolyelectrolyteβ-lactoglobulinComplexhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1In this work, the molecular interaction between the protein β-lactoglobulin and strong polyelectrolyte chains was studied using Monte Carlo simulations. Different coarse-grained models were used to represent the system components. Both net charge and protonation of the isolated dimeric protein were analyzed as a function of pH. The acid-base equilibrium of each titratable group was distinctively modified by the presence of polyanion or polycation chains. The complexation on the wrong side of pI was more evident with the polycation than with the polyanion. It was mainly due to a charge regulation mechanism, where the reversion in net charge of the protein was more pronounced at the left of isoelectric point of the protein. The glutamic and aspartic groups play a key role in this charge reversion. Both polyanion and polycation were spatially adsorbed in different region on the protein surface, suggesting the importance of the surface charge distribution of the protein.Fil: Torres, Paola Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; ArgentinaFil: Bojanich, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Sanchez Varretti, Fabricio Orlando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; ArgentinaFil: Ramirez Pastor, Antonio Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; ArgentinaFil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; ArgentinaFil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; ArgentinaFil: Narambuena, Claudio Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; ArgentinaElsevier Science2017-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/44507Torres, Paola Beatriz; Bojanich, Luciano; Sanchez Varretti, Fabricio Orlando; Ramirez Pastor, Antonio Jose; Quiroga, Evelina; et al.; Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 160; 12-2017; 161-1680927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927776517305933info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2017.09.018info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:47:48Zoai:ri.conicet.gov.ar:11336/44507instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:47:48.765CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
title Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
spellingShingle Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
Torres, Paola Beatriz
Whey proteins
Polyelectrolyte
β-lactoglobulin
Complex
title_short Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
title_full Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
title_fullStr Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
title_full_unstemmed Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
title_sort Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation
dc.creator.none.fl_str_mv Torres, Paola Beatriz
Bojanich, Luciano
Sanchez Varretti, Fabricio Orlando
Ramirez Pastor, Antonio Jose
Quiroga, Evelina
Boeris, Valeria
Narambuena, Claudio Fabian
author Torres, Paola Beatriz
author_facet Torres, Paola Beatriz
Bojanich, Luciano
Sanchez Varretti, Fabricio Orlando
Ramirez Pastor, Antonio Jose
Quiroga, Evelina
Boeris, Valeria
Narambuena, Claudio Fabian
author_role author
author2 Bojanich, Luciano
Sanchez Varretti, Fabricio Orlando
Ramirez Pastor, Antonio Jose
Quiroga, Evelina
Boeris, Valeria
Narambuena, Claudio Fabian
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Whey proteins
Polyelectrolyte
β-lactoglobulin
Complex
topic Whey proteins
Polyelectrolyte
β-lactoglobulin
Complex
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In this work, the molecular interaction between the protein β-lactoglobulin and strong polyelectrolyte chains was studied using Monte Carlo simulations. Different coarse-grained models were used to represent the system components. Both net charge and protonation of the isolated dimeric protein were analyzed as a function of pH. The acid-base equilibrium of each titratable group was distinctively modified by the presence of polyanion or polycation chains. The complexation on the wrong side of pI was more evident with the polycation than with the polyanion. It was mainly due to a charge regulation mechanism, where the reversion in net charge of the protein was more pronounced at the left of isoelectric point of the protein. The glutamic and aspartic groups play a key role in this charge reversion. Both polyanion and polycation were spatially adsorbed in different region on the protein surface, suggesting the importance of the surface charge distribution of the protein.
Fil: Torres, Paola Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
Fil: Bojanich, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Sanchez Varretti, Fabricio Orlando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
Fil: Ramirez Pastor, Antonio Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina
Fil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina
Fil: Narambuena, Claudio Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada ; Argentina. Universidad Tecnologica Nacional. Facultad Regional San Rafael; Argentina
description In this work, the molecular interaction between the protein β-lactoglobulin and strong polyelectrolyte chains was studied using Monte Carlo simulations. Different coarse-grained models were used to represent the system components. Both net charge and protonation of the isolated dimeric protein were analyzed as a function of pH. The acid-base equilibrium of each titratable group was distinctively modified by the presence of polyanion or polycation chains. The complexation on the wrong side of pI was more evident with the polycation than with the polyanion. It was mainly due to a charge regulation mechanism, where the reversion in net charge of the protein was more pronounced at the left of isoelectric point of the protein. The glutamic and aspartic groups play a key role in this charge reversion. Both polyanion and polycation were spatially adsorbed in different region on the protein surface, suggesting the importance of the surface charge distribution of the protein.
publishDate 2017
dc.date.none.fl_str_mv 2017-12
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/11336/44507
Torres, Paola Beatriz; Bojanich, Luciano; Sanchez Varretti, Fabricio Orlando; Ramirez Pastor, Antonio Jose; Quiroga, Evelina; et al.; Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 160; 12-2017; 161-168
0927-7765
CONICET Digital
CONICET
url http://hdl.handle.net/11336/44507
identifier_str_mv Torres, Paola Beatriz; Bojanich, Luciano; Sanchez Varretti, Fabricio Orlando; Ramirez Pastor, Antonio Jose; Quiroga, Evelina; et al.; Protonation of β-lactoglobulin in the presence of strong polyelectrolyte chains: a study using Monte Carlo simulation; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 160; 12-2017; 161-168
0927-7765
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927776517305933
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2017.09.018
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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