Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Physics |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-97332004000100009 |
Resumo: | The influence that urea has on the conformation of water-soluble globular protein, bovine serum albumin (BSA), exposed directly to the aqueous solution as compared to the condition where the macromolecule is confined in the Aerosol-OT (AOT - sodium bis-2-ethylhexyl sulfosuccinate)/n-hexane/water reverse micelle (RM) is addressed. Small angle X-ray scattering (SAXS), tryptophan (Trp) fluorescence emission and circular dichroism (CD) spectra of aqueous BSA solution in the absence and in the presence of urea (3M and 5M) confirm the known denaturating effect of urea in proteins. The loss of the globular native structure is observed by the increase in the protein maximum dimension and gyration radius, through the Trp emission increase and maximum red-shift as well as the decrease in alpha-helix content. In RMs, the Trp fluorescence and CD spectra show that BSA is mainly located in its interfacial region independently of the micellar size. Addition of urea in this BSA/RM system also causes changes in the Trp fluorescence (emission decrease and maximum red-shift) and in the BSA CD spectra (decrease in alpha-helix content), which are compatible with the denaturation of the protein and Trp exposition to a more apolar environment in the RM. The fact that urea causes changes in the protein structure when it is located in the interfacial region (evidenced by CD) is interpreted as an indication that the direct interaction of urea with the protein is the major factor to explain its denaturating effect. |
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Brazilian Journal of Physics |
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Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroismThe influence that urea has on the conformation of water-soluble globular protein, bovine serum albumin (BSA), exposed directly to the aqueous solution as compared to the condition where the macromolecule is confined in the Aerosol-OT (AOT - sodium bis-2-ethylhexyl sulfosuccinate)/n-hexane/water reverse micelle (RM) is addressed. Small angle X-ray scattering (SAXS), tryptophan (Trp) fluorescence emission and circular dichroism (CD) spectra of aqueous BSA solution in the absence and in the presence of urea (3M and 5M) confirm the known denaturating effect of urea in proteins. The loss of the globular native structure is observed by the increase in the protein maximum dimension and gyration radius, through the Trp emission increase and maximum red-shift as well as the decrease in alpha-helix content. In RMs, the Trp fluorescence and CD spectra show that BSA is mainly located in its interfacial region independently of the micellar size. Addition of urea in this BSA/RM system also causes changes in the Trp fluorescence (emission decrease and maximum red-shift) and in the BSA CD spectra (decrease in alpha-helix content), which are compatible with the denaturation of the protein and Trp exposition to a more apolar environment in the RM. The fact that urea causes changes in the protein structure when it is located in the interfacial region (evidenced by CD) is interpreted as an indication that the direct interaction of urea with the protein is the major factor to explain its denaturating effect.Sociedade Brasileira de Física2004-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-97332004000100009Brazilian Journal of Physics v.34 n.1 2004reponame:Brazilian Journal of Physicsinstname:Sociedade Brasileira de Física (SBF)instacron:SBF10.1590/S0103-97332004000100009info:eu-repo/semantics/openAccessItri,RosangelaCaetano,WilkerBarbosa,Leandro R. S.Baptista,Mauricio S.eng2004-04-27T00:00:00Zoai:scielo:S0103-97332004000100009Revistahttp://www.sbfisica.org.br/v1/home/index.php/pt/ONGhttps://old.scielo.br/oai/scielo-oai.phpsbfisica@sbfisica.org.br||sbfisica@sbfisica.org.br1678-44480103-9733opendoar:2004-04-27T00:00Brazilian Journal of Physics - Sociedade Brasileira de Física (SBF)false |
dc.title.none.fl_str_mv |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
title |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
spellingShingle |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism Itri,Rosangela |
title_short |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
title_full |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
title_fullStr |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
title_full_unstemmed |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
title_sort |
Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
author |
Itri,Rosangela |
author_facet |
Itri,Rosangela Caetano,Wilker Barbosa,Leandro R. S. Baptista,Mauricio S. |
author_role |
author |
author2 |
Caetano,Wilker Barbosa,Leandro R. S. Baptista,Mauricio S. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Itri,Rosangela Caetano,Wilker Barbosa,Leandro R. S. Baptista,Mauricio S. |
description |
The influence that urea has on the conformation of water-soluble globular protein, bovine serum albumin (BSA), exposed directly to the aqueous solution as compared to the condition where the macromolecule is confined in the Aerosol-OT (AOT - sodium bis-2-ethylhexyl sulfosuccinate)/n-hexane/water reverse micelle (RM) is addressed. Small angle X-ray scattering (SAXS), tryptophan (Trp) fluorescence emission and circular dichroism (CD) spectra of aqueous BSA solution in the absence and in the presence of urea (3M and 5M) confirm the known denaturating effect of urea in proteins. The loss of the globular native structure is observed by the increase in the protein maximum dimension and gyration radius, through the Trp emission increase and maximum red-shift as well as the decrease in alpha-helix content. In RMs, the Trp fluorescence and CD spectra show that BSA is mainly located in its interfacial region independently of the micellar size. Addition of urea in this BSA/RM system also causes changes in the Trp fluorescence (emission decrease and maximum red-shift) and in the BSA CD spectra (decrease in alpha-helix content), which are compatible with the denaturation of the protein and Trp exposition to a more apolar environment in the RM. The fact that urea causes changes in the protein structure when it is located in the interfacial region (evidenced by CD) is interpreted as an indication that the direct interaction of urea with the protein is the major factor to explain its denaturating effect. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-03-01 |
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=S0103-97332004000100009 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-97332004000100009 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-97332004000100009 |
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 Física |
publisher.none.fl_str_mv |
Sociedade Brasileira de Física |
dc.source.none.fl_str_mv |
Brazilian Journal of Physics v.34 n.1 2004 reponame:Brazilian Journal of Physics instname:Sociedade Brasileira de Física (SBF) instacron:SBF |
instname_str |
Sociedade Brasileira de Física (SBF) |
instacron_str |
SBF |
institution |
SBF |
reponame_str |
Brazilian Journal of Physics |
collection |
Brazilian Journal of Physics |
repository.name.fl_str_mv |
Brazilian Journal of Physics - Sociedade Brasileira de Física (SBF) |
repository.mail.fl_str_mv |
sbfisica@sbfisica.org.br||sbfisica@sbfisica.org.br |
_version_ |
1754734860502564864 |