Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

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dc.contributor.authorBatista, Andrea N. L. [UNESP]
dc.contributor.authorBatista, Joao M. [UNESP]
dc.contributor.authorAshton, Lorna
dc.contributor.authorBolzani, Vanderlan da Silva [UNESP]
dc.contributor.authorFurlan, Maysa [UNESP]
dc.contributor.authorBlanch, Ewan W.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Manchester
dc.date.accessioned2015-03-18T15:52:32Z
dc.date.available2015-03-18T15:52:32Z
dc.date.issued2014-09-01
dc.description.abstractRecent Raman and Raman optical activity (ROA) results have demonstrated that dimethyl sulfoxide (DMSO) induces the selective conversion of alpha-helix motifs into the poly(L-proline) II (PPII) helix conformation in an array of proteins, while beta-sheets remain mostly unaffected. Human serum albumin (HSA), a highly alpha-helical protein, underwent the most dramatic changes and, therefore, was selected as a model for further investigations into the mechanism of this conformational change. Herein we report the use of two-dimensional ROA correlation analysis applying synchronous, autocorrelation, and moving windows approaches in order to understand the conformational transitions in HSA as a function of DMSO concentration. Our results indicate that the destabilization of native alpha-helix starts at DMSO concentrations as little as 20% in water (v/v), with the transition to PPII helix being complete at similar to 80% DMSO. These results clearly indicate that any protein preparation containing relatively low concentrations of DMSO should consider possible disruptions in alpha-helical domains. (C) 2014 Wiley Periodicals, Inc.en
dc.description.affiliationUniv Estadual Paulista UNESP, Inst Quim, Dept Quim Organ, BR-14800060 Araraquara, SP, Brazil
dc.description.affiliationUniv Manchester, Manchester Inst Biotechnol, Manchester, Lancs, England
dc.description.affiliationUniv Manchester, Fac Life Sci, Manchester, Lancs, England
dc.description.affiliationUniv Manchester, Sch Chem, Manchester, Lancs, England
dc.description.affiliationUnespUniv Estadual Paulista UNESP, Inst Quim, Dept Quim Organ, BR-14800060 Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipManchester Chemical Biology Network (MCBN)
dc.description.sponsorshipIdFAPESP: 13/07600-3
dc.description.sponsorshipIdFAPESP: 12/16484-4
dc.description.sponsorshipIdFAPESP: 12/13739-1
dc.format.extent497-501
dc.identifierhttp://dx.doi.org/10.1002/chir.22351
dc.identifier.citationChirality. Hoboken: Wiley-blackwell, v. 26, n. 9, p. 497-501, 2014.
dc.identifier.doi10.1002/chir.22351
dc.identifier.issn0899-0042
dc.identifier.lattes4484083685251673
dc.identifier.lattes1308042794786872
dc.identifier.urihttp://hdl.handle.net/11449/116181
dc.identifier.wosWOS:000343295600011
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofChirality
dc.relation.ispartofjcr1.833
dc.relation.ispartofsjr0,536
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectROAen
dc.subject2DCOSen
dc.subjectHSAen
dc.subjectmoving windowsen
dc.subjectproteinen
dc.subjectsecondary structureen
dc.subjectPPII helixen
dc.titleInvestigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopyen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-Blackwell
unesp.author.lattes4484083685251673
unesp.author.lattes1308042794786872
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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