Tertiary structural changes of the alpha-hemolysin from Staphylococcus aureus on association with liposome membranes

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dc.contributor.authorBortoleto, R. K.
dc.contributor.authorde Oliveira, AHC
dc.contributor.authorRuller, R.
dc.contributor.authorArni, R. K.
dc.contributor.authorWard, R. J.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:19Z
dc.date.available2014-05-20T14:02:19Z
dc.date.issued1998-03-01
dc.description.abstractThe interaction of alpha-hemolysin (also called alpha-toxin) from Staphylococcus aureus with mixed egg-yolk phosphatidylcholine/cholesterol liposomes has been investigated using the intrinsic tryptophan fluorescence emission (ITFE) signal. The ITFE intensity of alpha-hemolysin, which was obtained using a novel purification protocol, showed a triphasic increase on incubation with liposomes at low protein/lipid ratios. The first, rapid phase results in an increase in ITFE of 10%, which reflects rapid conformation changes in the alpha-hemolysin on association with the liposome membrane, the second phase of the ITFE increase is associated with a red shift from 334 to 339 nm in the maximum emission wavelength, suggesting the transition to a partially unfolded intermediate in the oligomerization process. The third phase of the ITFE intensity change demonstrates a temporal correlation with the appearance of SDS-stable oligomers. The results demonstrate the feasibility of identification of intermediate protein conformations in complex membrane-associated processes by manipulation of the liposomal membrane composition. (C) 1998 Academic Press.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, Biol Struct Grp, BR-15054600 Sao Jose Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, Biol Struct Grp, BR-15054600 Sao Jose Rio Preto, SP, Brazil
dc.format.extent47-52
dc.identifierhttp://dx.doi.org/10.1006/abbi.1997.0550
dc.identifier.citationArchives of Biochemistry and Biophysics. San Diego: Academic Press Inc., v. 351, n. 1, p. 47-52, 1998.
dc.identifier.doi10.1006/abbi.1997.0550
dc.identifier.issn0003-9861
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21966
dc.identifier.wosWOS:000072310900007
dc.language.isoeng
dc.publisherAcademic Press Inc.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.ispartofjcr3.118
dc.relation.ispartofsjr1,350
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectalpha-hemolysinpt
dc.subjectalpha-toxinpt
dc.subjectStaphylococcus aureuspt
dc.subjectpore-formingpt
dc.subjectliposome membranept
dc.subjectunfolded intermediatept
dc.titleTertiary structural changes of the alpha-hemolysin from Staphylococcus aureus on association with liposome membranesen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderAcademic Press Inc.
unesp.author.lattes9162508978945887[4]
unesp.author.orcid0000-0003-2460-1145[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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