Adsorption and protonation of peptides and proteins in pH responsive gels

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 c...

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Autores principales: Longo, Gabriel Sebastián, Szleifer, Igal
Formato: Articulo
Lenguaje:Inglés
Publicado: 2016
Materias:
Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/97952
https://ri.conicet.gov.ar/11336/62296
http://iopscience.iop.org/article/10.1088/0022-3727/49/32/323001/meta
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-97952
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
spellingShingle Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
Longo, Gabriel Sebastián
Szleifer, Igal
Adsorption and protonation of peptides and proteins in pH responsive gels
topic_facet Ciencias Exactas
Química
Acid-base equilibrium
Adsorption
Responsive gel
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.
format Articulo
Articulo
author Longo, Gabriel Sebastián
Szleifer, Igal
author_facet Longo, Gabriel Sebastián
Szleifer, Igal
author_sort Longo, Gabriel Sebastián
title Adsorption and protonation of peptides and proteins in pH responsive gels
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
publishDate 2016
url http://sedici.unlp.edu.ar/handle/10915/97952
https://ri.conicet.gov.ar/11336/62296
http://iopscience.iop.org/article/10.1088/0022-3727/49/32/323001/meta
work_keys_str_mv AT longogabrielsebastian adsorptionandprotonationofpeptidesandproteinsinphresponsivegels
AT szleiferigal adsorptionandprotonationofpeptidesandproteinsinphresponsivegels
bdutipo_str Repositorios
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