Investigation of Human Albumin-Induced Circular Dichroism in Dansylglycine

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dc.contributor.authorGraciani, Fernanda S. [UNESP]
dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-12-03T13:11:46Z
dc.date.available2014-12-03T13:11:46Z
dc.date.issued2013-10-16
dc.description.abstractInduced circular dichroism (ICD), or induced chirality, is a phenomenon caused by the fixation of an achiral substance inside a chiral microenvironment, such as the hydrophobic cavities in proteins. Dansylglycine belongs to a class of dansylated amino acids, which are largely used as fluorescent probes for the characterization of the binding sites in albumin. Here, we investigated the ICD in dansylglycine provoked by its binding to human serum albumin (HSA). We found that the complexation of HSA with dansylglycine resulted in the appearance of an ICD band centred at 346 nm. Using this ICD signal and site-specific ligands of HSA, we confirmed that dansylglycine is a site II ligand. The intensity of the ICD signal was dependent on the temperature and revealed that the complexation between the protein and the ligand was reversible. The induced chirality of dansylglycine was susceptive to the alteration caused by the oxidation of the protein. A comparison was made between hypochlorous acid (HOCl) and hypobromous acid (HOBr), and revealed that site II in the protein is more susceptible to alteration provoked by the latter oxidant. These findings suggest the relevance of the aromatic amino acids in the site II, since HOBr is a more efficient oxidant of these residues in proteins than HOCl. The three-dimensional structure of HSA is pH-dependent, and different conformations have been characterised. We found that HSA in its basic form at pH 9.0, which causes the protein to be less rigid, lost the capacity to bind dansylglycine. At pH 3.5, HSA retained almost all of its capacity for binding to dansylglycine. Since the structure of HSA at pH 3.5 is expanded, separating the domain IIIA from the rest of the molecule, we concluded that this separation did not alter its binding capacity to dansylglycine.en
dc.description.affiliationUniv Estadual Paulista, Dept Quim, Fac Ciencias, Bauru, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Quim, Fac Ciencias, Bauru, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 11/50652-9
dc.format.extent8
dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0076849
dc.identifier.citationPlos One. San Francisco: Public Library Science, v. 8, n. 10, 8 p., 2013.
dc.identifier.doi10.1371/journal.pone.0076849
dc.identifier.fileWOS000326019400088.pdf
dc.identifier.issn1932-6203
dc.identifier.lattes4066413997908572
dc.identifier.urihttp://hdl.handle.net/11449/113536
dc.identifier.wosWOS:000326019400088
dc.language.isoeng
dc.publisherPublic Library Science
dc.relation.ispartofPLOS ONE
dc.relation.ispartofjcr2.766
dc.relation.ispartofsjr1,164
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleInvestigation of Human Albumin-Induced Circular Dichroism in Dansylglycineen
dc.typeArtigo
dcterms.rightsHolderPublic Library Science
unesp.author.lattes4066413997908572
unesp.author.orcid0000-0003-2636-3080[2]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências, Baurupt
unesp.departmentQuímica - FCpt

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Bauru - FC - Faculdade de Ciências
Artigos - Análises Clínicas - FCFAR