dc.creatorPrates, MV
dc.creatorSforca, ML
dc.creatorRegis, WCB
dc.creatorLeite, JRSA
dc.creatorSilva, LP
dc.creatorPertinhez, TA
dc.creatorAraujo, ALT
dc.creatorAzevedo, RB
dc.creatorSpisni, A
dc.creatorBloch, C
dc.date2004
dc.date46082
dc.date2014-11-15T05:55:39Z
dc.date2015-11-26T16:09:33Z
dc.date2014-11-15T05:55:39Z
dc.date2015-11-26T16:09:33Z
dc.date.accessioned2018-03-28T22:58:08Z
dc.date.available2018-03-28T22:58:08Z
dc.identifierJournal Of Biological Chemistry. Amer Soc Biochemistry Molecular Biology Inc, v. 279, n. 13, n. 13018, n. 13026, 2004.
dc.identifier0021-9258
dc.identifierWOS:000220334900122
dc.identifier10.1074/jbc.M310838200
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/78187
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/78187
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/78187
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1266648
dc.descriptionAmphibian skin secretions constitute an important source of molecules for antimicrobial drug research in order to combat the increasing resistance of pathogens to conventional antibiotics. Among the various types of substances secreted by the dermal granular amphibian glands, there is a wide range of peptides and proteins, often displaying potent antimicrobial activities and providing an effective defense system against parasite infection. In the present work, we report the NMR solution structure and the biological activity of a cationic 14-residue amphiphilic alpha-helical polypeptide named Hylaseptin P1 ( HSP1), isolated from the skin secretion of the hylid frog Hyla punctata. The peptide antimicrobial activity was verified against Candida albicans, Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa, whereas no significant lytic effect was detected toward red or white blood cells.
dc.description279
dc.description13
dc.description13018
dc.description13026
dc.languageen
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.publisherBethesda
dc.publisherEUA
dc.relationJournal Of Biological Chemistry
dc.relationJ. Biol. Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectCross-relaxation
dc.subjectFrog-skin
dc.subjectSpectroscopy
dc.subjectCells
dc.subjectKetoconazole
dc.subjectAntibiotics
dc.subjectElucidation
dc.subjectInfections
dc.subjectPrecursor
dc.subjectProteins
dc.titleThe NMR-derived solution structure of a new cationic antimicrobial peptide from the skin secretion of the anuran Hyla punctata
dc.typeArtículos de revistas


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