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

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorBatista, Andrea N. L.-
Autor(es): dc.creatorBatista, Joao M.-
Autor(es): dc.creatorAshton, Lorna-
Autor(es): dc.creatorBolzani, Vanderlan da Silva-
Autor(es): dc.creatorFurlan, Maysa-
Autor(es): dc.creatorBlanch, Ewan W.-
Data de aceite: dc.date.accessioned2021-03-10T21:28:21Z-
Data de disponibilização: dc.date.available2021-03-10T21:28:21Z-
Data de envio: dc.date.issued2015-03-18-
Data de envio: dc.date.issued2015-03-18-
Data de envio: dc.date.issued2014-09-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/chir.22351-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/116181-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/116181-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionManchester Chemical Biology Network (MCBN)-
Descrição: dc.descriptionProcesso FAPESP: 13/07600-3-
Descrição: dc.descriptionProcesso FAPESP: 12/16484-4-
Descrição: dc.descriptionProcesso FAPESP: 12/13739-1-
Descrição: dc.descriptionRecent 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.-
Formato: dc.format497-501-
Idioma: dc.languageen-
Publicador: dc.publisherWiley-Blackwell-
Relação: dc.relationChirality-
Relação: dc.relation1.833-
Relação: dc.relation0,536-
Direitos: dc.rightsclosedAccess-
Palavras-chave: dc.subjectROA-
Palavras-chave: dc.subject2DCOS-
Palavras-chave: dc.subjectHSA-
Palavras-chave: dc.subjectmoving windows-
Palavras-chave: dc.subjectprotein-
Palavras-chave: dc.subjectsecondary structure-
Palavras-chave: dc.subjectPPII helix-
Título: dc.titleInvestigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy-
Tipo de arquivo: dc.typelivro digital-
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