Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/29357
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dc.contributor.authorMachado, Alessandra
dc.contributor.authorSforca, Mauricio L.
dc.contributor.authorMiranda, Antonio
dc.contributor.authorDaffre, Sirlei
dc.contributor.authorPertinhez, Thelma A.
dc.contributor.authorSpisni, Alberto
dc.contributor.authorMiranda, M. Teresa M.
dc.date.accessioned2016-01-24T12:41:43Z-
dc.date.available2016-01-24T12:41:43Z-
dc.date.issued2007-01-01
dc.identifierhttp://dx.doi.org/10.1002/bip.20688
dc.identifier.citationBiopolymers. Hoboken: John Wiley & Sons Inc, v. 88, n. 3, p. 413-426, 2007.
dc.identifier.issn0006-3525
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/29357-
dc.description.abstractPeptides derived from endogenous hemoglobin play important biological roles in a variety of living systems. in previous works we showed that the fragment 33-61 of bovine alpha=hemoglobin (Hb33-61) and its C-terminus amidated analogue (Hb33-61a) exhibit antimicrobial activity and we determined the 3D structure of HB33-61a bound to sodium dodecyl sulfate micelles. Here we report that Hb33-61a is lethal to Candida albicans at 625 mu M probably through disruption of its plasma membrane. in addition, we show that, even when used at 50 mu M, Hb33-61a produces low hemolysis (16% +/- 3.0%). Recognizing that one of the key steps to study new compounds with potential pharmaceutical application is to identify the structural elements essential to express biological activity, we also investigated the anticandidal activity of HB33-61a fragments. the results indicated that Hb40-61a exhibits the same minimal inhibitory concentration as Hb33-61a, whereas HB33-52a and Hb48-61a are significantly less astive. Noteworthy, for all the peptides tested, we observed that C-terminus amidation produces a potentiation of their anticandidal activity and we associate that increased biological activity and we associate that increased biological activity to a preferred structural and spatial organization of the C-terminal region favored by amidation. Finally, the data show that the most active peptides (Hb33-61a and Hb40-61a) are characterized by a central hinge joining the C-terminal region (containing a beta-turn followed by a helical element) to the N-terminal region (that presents only a beta-turn). We hypothesize that these two structured regions, by fluctuating independently in the lipid environment, may act in a coordinated fashion disrupting the yeast plasma membrane. (c) 2007 Wiley Periodicals, Inc.en
dc.format.extent413-426
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofBiopolymers
dc.rightsAcesso restrito
dc.subjectantimicrobial peptidesen
dc.subjectCandida albicansen
dc.subjectstructure-activity relationshipen
dc.subjectpeptide synthesisen
dc.subjectNMRen
dc.titleTruncation of amidated fragment 33-61 of bovine alpha-hemoglobin: Effects on the structure and anticandidal activityen
dc.typeArtigo
dc.rights.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionCtr Struct Mol Biol
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Parma
dc.description.affiliationUniv São Paulo, Inst Chem, Dept Biochem, São Paulo, Brazil
dc.description.affiliationCtr Struct Mol Biol, Brazilian Lab Synchrotron Light, Campinas, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Biomed Sci, Dept Parasitol, São Paulo, Brazil
dc.description.affiliationUniv Parma, Dept Expt Med, I-43100 Parma, Italy
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.identifier.doi10.1002/bip.20688
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000245937400008
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