Adsorption and protonation of peptides and proteins in pH responsive gels

Autores
Longo, Gabriel Sebastián; Szleifer, Igal
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
To describe the non-trivial features of the equilibrium protonation and physical adsorption of peptides/proteins in pH-responsive hydrogels, we summarize our recent theoretical work on the subject. In these systems, molecular confinement in nanometer-sized environments modifies the balance between chemical state, physical interactions and molecular organization, which results in a behavior that is qualitatively different from what is expected from assuming the bulk solution protonation. To enhance adsorption, the pH-dependent deprotonation curves of all amino acids of adsorbed proteins are adequately shifted and deformed, which depends, in a complex fashion, on the specific amino acid. This possibility of modifying different acid-base equilibriums gives the adsorbed protein degrees of freedom to regulate charge and enhance electrostatic attractions under a wide range of experimental conditions. Protein adsorption modifies the microenvironment inside the hydrogel, particularly the gel pH. As a result, the state of protonation of the network is different before and after adsorption. The physicochemical considerations described in this review can be useful in the design of functional materials involving protein adsorption.
Facultad de Ciencias Exactas
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/97952
Acceder
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network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Adsorption and protonation of peptides and proteins in pH responsive gelsLongo, Gabriel SebastiánSzleifer, IgalCiencias ExactasQuímicaAcid-base equilibriumAdsorptionResponsive gelTo describe the non-trivial features of the equilibrium protonation and physical adsorption of peptides/proteins in pH-responsive hydrogels, we summarize our recent theoretical work on the subject. In these systems, molecular confinement in nanometer-sized environments modifies the balance between chemical state, physical interactions and molecular organization, which results in a behavior that is qualitatively different from what is expected from assuming the bulk solution protonation. To enhance adsorption, the pH-dependent deprotonation curves of all amino acids of adsorbed proteins are adequately shifted and deformed, which depends, in a complex fashion, on the specific amino acid. This possibility of modifying different acid-base equilibriums gives the adsorbed protein degrees of freedom to regulate charge and enhance electrostatic attractions under a wide range of experimental conditions. Protein adsorption modifies the microenvironment inside the hydrogel, particularly the gel pH. As a result, the state of protonation of the network is different before and after adsorption. The physicochemical considerations described in this review can be useful in the design of functional materials involving protein adsorption.Facultad de Ciencias ExactasInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/97952enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/62296info:eu-repo/semantics/altIdentifier/url/http://iopscience.iop.org/article/10.1088/0022-3727/49/32/323001/metainfo:eu-repo/semantics/altIdentifier/issn/0022-3727info:eu-repo/semantics/altIdentifier/doi/10.1088/0022-3727/49/32/323001info:eu-repo/semantics/altIdentifier/hdl/11336/62296info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:12:10Zoai:sedici.unlp.edu.ar:10915/97952Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:12:10.414SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Adsorption and protonation of peptides and proteins in pH responsive gels
title Adsorption and protonation of peptides and proteins in pH responsive gels
spellingShingle Adsorption and protonation of peptides and proteins in pH responsive gels
Longo, Gabriel Sebastián
Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
title_short Adsorption and protonation of peptides and proteins in pH responsive gels
title_full Adsorption and protonation of peptides and proteins in pH responsive gels
title_fullStr Adsorption and protonation of peptides and proteins in pH responsive gels
title_full_unstemmed Adsorption and protonation of peptides and proteins in pH responsive gels
title_sort Adsorption and protonation of peptides and proteins in pH responsive gels
dc.creator.none.fl_str_mv Longo, Gabriel Sebastián
Szleifer, Igal
author Longo, Gabriel Sebastián
author_facet Longo, Gabriel Sebastián
Szleifer, Igal
author_role author
author2 Szleifer, Igal
author2_role author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
topic Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
dc.description.none.fl_txt_mv To describe the non-trivial features of the equilibrium protonation and physical adsorption of peptides/proteins in pH-responsive hydrogels, we summarize our recent theoretical work on the subject. In these systems, molecular confinement in nanometer-sized environments modifies the balance between chemical state, physical interactions and molecular organization, which results in a behavior that is qualitatively different from what is expected from assuming the bulk solution protonation. To enhance adsorption, the pH-dependent deprotonation curves of all amino acids of adsorbed proteins are adequately shifted and deformed, which depends, in a complex fashion, on the specific amino acid. This possibility of modifying different acid-base equilibriums gives the adsorbed protein degrees of freedom to regulate charge and enhance electrostatic attractions under a wide range of experimental conditions. Protein adsorption modifies the microenvironment inside the hydrogel, particularly the gel pH. As a result, the state of protonation of the network is different before and after adsorption. The physicochemical considerations described in this review can be useful in the design of functional materials involving protein adsorption.
Facultad de Ciencias Exactas
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description To describe the non-trivial features of the equilibrium protonation and physical adsorption of peptides/proteins in pH-responsive hydrogels, we summarize our recent theoretical work on the subject. In these systems, molecular confinement in nanometer-sized environments modifies the balance between chemical state, physical interactions and molecular organization, which results in a behavior that is qualitatively different from what is expected from assuming the bulk solution protonation. To enhance adsorption, the pH-dependent deprotonation curves of all amino acids of adsorbed proteins are adequately shifted and deformed, which depends, in a complex fashion, on the specific amino acid. This possibility of modifying different acid-base equilibriums gives the adsorbed protein degrees of freedom to regulate charge and enhance electrostatic attractions under a wide range of experimental conditions. Protein adsorption modifies the microenvironment inside the hydrogel, particularly the gel pH. As a result, the state of protonation of the network is different before and after adsorption. The physicochemical considerations described in this review can be useful in the design of functional materials involving protein adsorption.
publishDate 2016
dc.date.none.fl_str_mv 2016-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/97952
url http://sedici.unlp.edu.ar/handle/10915/97952
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/62296
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info:eu-repo/semantics/altIdentifier/issn/0022-3727
info:eu-repo/semantics/altIdentifier/doi/10.1088/0022-3727/49/32/323001
info:eu-repo/semantics/altIdentifier/hdl/11336/62296
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
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reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.22299

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