A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus

Detalhes bibliográficos
Autor(a) principal: Bortoleto, R. K.
Data de Publicação: 1999
Outros Autores: Ward, R. J.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/S0014-5793(99)01246-6
http://hdl.handle.net/11449/21976
Resumo: The effects of mildly acidic conditions on the free energy of unfolding (Delta G(u)(buff)) of the pore-forming alpha-hemolysin (alpha HL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation, Decreasing the pH from 7.0 to 5.0 reduced the calculated Delta G(u)(buff) from 8.9 to 4.2 kcal moI(-1), which correlates with an increased rate of pore formation previously observed over the same pH range, It is proposed that the lowered surface pH of biological membranes reduces the stability of alpha HL thereby modulating the rate of pore formation. (C) 1999 Federation of European Biochemical Societies.
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spelling A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureusalpha-hemolysinstability transitionThe effects of mildly acidic conditions on the free energy of unfolding (Delta G(u)(buff)) of the pore-forming alpha-hemolysin (alpha HL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation, Decreasing the pH from 7.0 to 5.0 reduced the calculated Delta G(u)(buff) from 8.9 to 4.2 kcal moI(-1), which correlates with an increased rate of pore formation previously observed over the same pH range, It is proposed that the lowered surface pH of biological membranes reduces the stability of alpha HL thereby modulating the rate of pore formation. (C) 1999 Federation of European Biochemical Societies.USP, FFCLRP, Dept Chem, Ribeirao Preto, SP, BrazilUNESP, IBILCE, Dept Phys, Sao Jose Rio Preto, SP, BrazilUNESP, IBILCE, Dept Phys, Sao Jose Rio Preto, SP, BrazilElsevier B.V.Universidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Bortoleto, R. K.Ward, R. J.2014-05-20T14:02:21Z2014-05-20T14:02:21Z1999-10-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article438-442application/pdfhttp://dx.doi.org/10.1016/S0014-5793(99)01246-6Febs Letters. Amsterdam: Elsevier B.V., v. 459, n. 3, p. 438-442, 1999.0014-5793http://hdl.handle.net/11449/2197610.1016/S0014-5793(99)01246-6WOS:000083204500030WOS000083204500030.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengFEBS Letters1,991info:eu-repo/semantics/openAccess2023-11-26T06:14:56Zoai:repositorio.unesp.br:11449/21976Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:47:59.954601Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
title A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
spellingShingle A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
Bortoleto, R. K.
alpha-hemolysin
stability transition
title_short A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
title_full A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
title_fullStr A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
title_full_unstemmed A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
title_sort A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
author Bortoleto, R. K.
author_facet Bortoleto, R. K.
Ward, R. J.
author_role author
author2 Ward, R. J.
author2_role author
dc.contributor.none.fl_str_mv Universidade de São Paulo (USP)
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Bortoleto, R. K.
Ward, R. J.
dc.subject.por.fl_str_mv alpha-hemolysin
stability transition
topic alpha-hemolysin
stability transition
description The effects of mildly acidic conditions on the free energy of unfolding (Delta G(u)(buff)) of the pore-forming alpha-hemolysin (alpha HL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation, Decreasing the pH from 7.0 to 5.0 reduced the calculated Delta G(u)(buff) from 8.9 to 4.2 kcal moI(-1), which correlates with an increased rate of pore formation previously observed over the same pH range, It is proposed that the lowered surface pH of biological membranes reduces the stability of alpha HL thereby modulating the rate of pore formation. (C) 1999 Federation of European Biochemical Societies.
publishDate 1999
dc.date.none.fl_str_mv 1999-10-15
2014-05-20T14:02:21Z
2014-05-20T14:02:21Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/S0014-5793(99)01246-6
Febs Letters. Amsterdam: Elsevier B.V., v. 459, n. 3, p. 438-442, 1999.
0014-5793
http://hdl.handle.net/11449/21976
10.1016/S0014-5793(99)01246-6
WOS:000083204500030
WOS000083204500030.pdf
url http://dx.doi.org/10.1016/S0014-5793(99)01246-6
http://hdl.handle.net/11449/21976
identifier_str_mv Febs Letters. Amsterdam: Elsevier B.V., v. 459, n. 3, p. 438-442, 1999.
0014-5793
10.1016/S0014-5793(99)01246-6
WOS:000083204500030
WOS000083204500030.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv FEBS Letters
1,991
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 438-442
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808128981491253248

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