Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , |
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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Journal of the Brazilian Chemical Society (Online) |
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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 |
_version_ |
1750318167791501312 |