dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2015-03-18T15:53:00Z
dc.date.available2015-03-18T15:53:00Z
dc.date.created2015-03-18T15:53:00Z
dc.date.issued2014-11-01
dc.identifierAmino Acids. Wien: Springer Wien, v. 46, n. 11, p. 2627-2631, 2014.
dc.identifier0939-4451
dc.identifierhttp://hdl.handle.net/11449/116279
dc.identifier10.1007/s00726-014-1832-x
dc.identifierWOS:000343995600016
dc.identifier0000-0002-4767-0904
dc.description.abstractWe have previously described the structure and the ability of a dimeric analog of the antimicrobial peptide Aurein 1.2 to aggregate Candida albicans. In this study, circular dichroism and fluorescence spectroscopy data showed that this aggregation is related to the interaction between the peptide and mannans, the main component of yeast cell wall. In this context, we propose a model in which dimers interact with the polysaccharide leading to cells aggregation.
dc.languageeng
dc.publisherSpringer
dc.relationAmino Acids
dc.relation2.906
dc.relation1,135
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectAurein 1.2
dc.subjectDimerization
dc.subjectCandida albicans
dc.subjectAggregation
dc.subjectMannans
dc.titleInteraction between the antimicrobial peptide Aurein 1.2 dimer and mannans
dc.typeArtículos de revistas


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