Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions

Detalhes bibliográficos
Autor(a) principal: Moreira,Livia A.
Data de Publicação: 2007
Outros Autores: Boström,Mathias, Ninham,Barry W., Biscaia,Evaristo C., Tavares,Frederico W.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Journal of the Brazilian Chemical Society (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532007000100026
Resumo: Interactions between proteins are studied by calculating the potential of mean force based on the Poisson-Boltzmann equation. We define a parameter that allows a comparison between the osmotic second virial coefficients obtained from different experimental analytical techniques and provides information about both protein-protein or protein-surface interactions. It can be related to the protein solubility and be used to determine favorable conditions for protein adsorption on a specific surface or protein aggregation. The calculations show reasonable agreement with the experimental second virial coefficient. They also reveal that it is possible to predict different Hofmeister effects observed experimentally in protein solutions. We demonstrate that the effect of including many-body ion-protein dispersion potentials originating from polarizabilities of ions and proteins may offer an explanation for the Hofmeister series. In particular, we give evidence for the inversion of Hofmeister series as function of pH for a given protein.
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spelling Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactionsvan der Waals interactionsHofmeister seriesprotein adsorptionosmotic second virial coefficientInteractions between proteins are studied by calculating the potential of mean force based on the Poisson-Boltzmann equation. We define a parameter that allows a comparison between the osmotic second virial coefficients obtained from different experimental analytical techniques and provides information about both protein-protein or protein-surface interactions. It can be related to the protein solubility and be used to determine favorable conditions for protein adsorption on a specific surface or protein aggregation. The calculations show reasonable agreement with the experimental second virial coefficient. They also reveal that it is possible to predict different Hofmeister effects observed experimentally in protein solutions. We demonstrate that the effect of including many-body ion-protein dispersion potentials originating from polarizabilities of ions and proteins may offer an explanation for the Hofmeister series. In particular, we give evidence for the inversion of Hofmeister series as function of pH for a given protein.Sociedade Brasileira de Química2007-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532007000100026Journal of the Brazilian Chemical Society v.18 n.1 2007reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532007000100026info:eu-repo/semantics/openAccessMoreira,Livia A.Boström,MathiasNinham,Barry W.Biscaia,Evaristo C.Tavares,Frederico W.eng2007-03-23T00:00:00Zoai:scielo:S0103-50532007000100026Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2007-03-23T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
title Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
spellingShingle Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
Moreira,Livia A.
van der Waals interactions
Hofmeister series
protein adsorption
osmotic second virial coefficient
title_short Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
title_full Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
title_fullStr Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
title_full_unstemmed Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
title_sort Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
author Moreira,Livia A.
author_facet Moreira,Livia A.
Boström,Mathias
Ninham,Barry W.
Biscaia,Evaristo C.
Tavares,Frederico W.
author_role author
author2 Boström,Mathias
Ninham,Barry W.
Biscaia,Evaristo C.
Tavares,Frederico W.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Moreira,Livia A.
Boström,Mathias
Ninham,Barry W.
Biscaia,Evaristo C.
Tavares,Frederico W.
dc.subject.por.fl_str_mv van der Waals interactions
Hofmeister series
protein adsorption
osmotic second virial coefficient
topic van der Waals interactions
Hofmeister series
protein adsorption
osmotic second virial coefficient
description Interactions between proteins are studied by calculating the potential of mean force based on the Poisson-Boltzmann equation. We define a parameter that allows a comparison between the osmotic second virial coefficients obtained from different experimental analytical techniques and provides information about both protein-protein or protein-surface interactions. It can be related to the protein solubility and be used to determine favorable conditions for protein adsorption on a specific surface or protein aggregation. The calculations show reasonable agreement with the experimental second virial coefficient. They also reveal that it is possible to predict different Hofmeister effects observed experimentally in protein solutions. We demonstrate that the effect of including many-body ion-protein dispersion potentials originating from polarizabilities of ions and proteins may offer an explanation for the Hofmeister series. In particular, we give evidence for the inversion of Hofmeister series as function of pH for a given protein.
publishDate 2007
dc.date.none.fl_str_mv 2007-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532007000100026
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532007000100026
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0103-50532007000100026
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Journal of the Brazilian Chemical Society v.18 n.1 2007
reponame:Journal of the Brazilian Chemical Society (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Journal of the Brazilian Chemical Society (Online)
collection Journal of the Brazilian Chemical Society (Online)
repository.name.fl_str_mv Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv ||office@jbcs.sbq.org.br
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