Dimerization of aurein 1.2: Effects in structure, antimicrobial activity and aggregation of Cândida albicans cells

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dc.contributor.authorLorenzón, E. N. [UNESP]
dc.contributor.authorSanches, P. R S [UNESP]
dc.contributor.authorNogueira, L. G. [UNESP]
dc.contributor.authorBauab, T. M. [UNESP]
dc.contributor.authorCilli, Eduardo Maffud [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:29:33Z
dc.date.available2014-05-27T11:29:33Z
dc.date.issued2013-06-01
dc.description.abstractAntimicrobial peptides (AMPs) are a promising solution to face the antibiotic-resistant problem because they display little or no resistance effects. Dimeric analogues of select AMPs have shown pharmacotechnical advantages, making these molecules promising candidates for the development of novel antibiotic agents. Here, we evaluate the effects of dimerization on the structure and biological activity of the AMP aurein 1.2 (AU). AU and the C- and N-terminal dimers, (AU)2K and E(AU)2, respectively, were synthesized by solid-phase peptide synthesis. Circular dichroism spectra indicated that E(AU)2 has a coiled coil structure in water while (AU)2K has an α-helix structure. In contrast, AU displayed typical spectra for disordered structures. In LPC micelles, all peptides acquired a high amount of α-helix structure. Hemolytic and vesicle permeabilization assays showed that AU has a concentration dependence activity, while this effect was less pronounced for dimeric versions, suggesting that dimerization may change the mechanism of action of AU. Notably, the antimicrobial activity against bacteria and yeast decreased with dimerization. However, dimeric peptides promoted the aggregation of C. albicans. The ability to aggregate yeast cells makes dimeric versions of AU attractive candidates to inhibit the adhesion of C. albicans to biological targets and medical devices, preventing disease caused by this fungus. © 2013 Springer-Verlag Wien.en
dc.description.affiliationInstitute of Chemistry University Estadual Paulista Araraquara (UNESP), Araraquara SP
dc.description.affiliationFaculty of Pharmaceutical Sciences University Estadual Paulista (UNESP), Araraquara SP
dc.description.affiliationUnespInstitute of Chemistry University Estadual Paulista Araraquara (UNESP), Araraquara SP
dc.description.affiliationUnespFaculty of Pharmaceutical Sciences University Estadual Paulista (UNESP), Araraquara SP
dc.format.extent1521-1528
dc.identifierhttp://dx.doi.org/10.1007/s00726-013-1475-3
dc.identifier.citationAmino Acids, v. 44, n. 6, p. 1521-1528, 2013.
dc.identifier.doi10.1007/s00726-013-1475-3
dc.identifier.issn0939-4451
dc.identifier.issn1438-2199
dc.identifier.lattes9424346762460416
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.scopus2-s2.0-84878221033
dc.identifier.urihttp://hdl.handle.net/11449/75476
dc.identifier.wosWOS:000319016900011
dc.language.isoeng
dc.relation.ispartofAmino Acids
dc.relation.ispartofjcr2.906
dc.relation.ispartofsjr1,135
dc.relation.ispartofsjr1,135
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectAntimicrobial peptides
dc.subjectAurein 1.2
dc.subjectBiological activity
dc.subjectDimerization
dc.subjectSecondary structure
dc.subjectaurein 1.2
dc.subjectlysophosphatidylcholine
dc.subjectpolypeptide antibiotic agent
dc.subjectunclassified drug
dc.subjectalpha helix
dc.subjectamino terminal sequence
dc.subjectantibacterial activity
dc.subjectantifungal activity
dc.subjectantimicrobial activity
dc.subjectCandida albicans
dc.subjectcarboxy terminal sequence
dc.subjectcell aggregation
dc.subjectcell permeabilization
dc.subjectcell vacuole
dc.subjectcircular dichroism
dc.subjectconcentration response
dc.subjectcontrolled study
dc.subjectdimerization
dc.subjectfungal cell
dc.subjecthemolysis
dc.subjecthuman
dc.subjecthuman cell
dc.subjectmicelle
dc.subjectmicrobial adhesion
dc.subjectminimum inhibitory concentration
dc.subjectnonhuman
dc.subjectpeptide synthesis
dc.subjectpriority journal
dc.subjectprotein function
dc.subjectprotein structure
dc.subjectsolid phase synthesis
dc.subjectFungi
dc.titleDimerization of aurein 1.2: Effects in structure, antimicrobial activity and aggregation of Cândida albicans cellsen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights
unesp.author.lattes9424346762460416
unesp.author.orcid0000-0002-4767-0904[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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