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An ultraviolet photoacoustic spectroscopy study of the interaction between Lys49-phospholipase A(2) and amphiphilic molecules

dc.contributor.authorBugs, Milton Roque
dc.contributor.authorBortoleto-Bugs, Raquel Kely
dc.contributor.authorCornelio, Marinonio Lopes
dc.contributor.authorWard, Richard John
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T14:02:25Z
dc.date.available2014-05-20T14:02:25Z
dc.date.issued2007-02-23
dc.description.abstractWe have used near ultraviolet photoacoustic spectroscopy (PAS) over the wavelength range 240-320 nm to investigate the complex formed between the homodimeric bothropstoxin-I, a lysine-49-phospholipase A(2) from the venom of Bothrops jararacussu (BthTx-I), with the anionic amphiphile sodium dodecyl sulfate (SDS). At molar ratios > 10, the complex developed a significant light scatter, accompanied by a decrease in the intrinsic tryptophan fluorescence intensity emission (ITFE) of the protein, and an increase in the near UV-PAS signal. Difference PAS spectroscopy at SDS/BthTx-I ratios < 8 were limited to the region 280-290 nm, suggesting initial SDS binding to the tryptophan 77 located at the dimer interface. At SDS/BthTx-I ratios > 10, the intensity between 260 and 320 nm increases demonstrating that the more widespread tyrosine and phenylalanine residues contribute to the SDS/BthTx-I interaction. PAS signal phase changes at wavelengths specific for each aromatic residue suggest that the Trp77 becomes more buried on SDS binding, and that protein structural changes and dehydration may alter the microenvironments of Tyr and Phe residues. These results demonstrate the potential of near UV-PAS for the investigation of membrane proteins/detergent complexes in which light scatter is significant. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, IBILCE, Dept Phys, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Fac Filosofia Ciências & Letras Ribeirao Pret, Dept Chem, BR-14049901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, Sao Jose do Rio Preto, SP, Brazil
dc.format.extent889-894
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2006.12.085
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 353, n. 4, p. 889-894, 2007.
dc.identifier.doi10.1016/j.bbrc.2006.12.085
dc.identifier.issn0006-291X
dc.identifier.lattes3874425691257843
dc.identifier.urihttp://hdl.handle.net/11449/22008
dc.identifier.wosWOS:000243859600008
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.relation.ispartofjcr2.559
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectphotoacoustic spectroscopypt
dc.subjectbothropstoxin-Ipt
dc.subjectdifference spectroscopypt
dc.subjectfluorescencept
dc.titleAn ultraviolet photoacoustic spectroscopy study of the interaction between Lys49-phospholipase A(2) and amphiphilic moleculesen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes3874425691257843
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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