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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/34191
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dc.contributor.authorCastro, Mariana S.-
dc.contributor.authorCilli, Eduardo Maffud-
dc.contributor.authorFontes, Wagner-
dc.date.accessioned2014-05-20T15:23:24Z-
dc.date.accessioned2016-10-25T17:57:20Z-
dc.date.available2014-05-20T15:23:24Z-
dc.date.available2016-10-25T17:57:20Z-
dc.date.issued2006-12-01-
dc.identifierhttp://dx.doi.org/10.2174/138920306779025648-
dc.identifier.citationCurrent Protein & Peptide Science. Sharjah: Bentham Science Publ Ltd, v. 7, n. 6, p. 473-478, 2006.-
dc.identifier.issn1389-2037-
dc.identifier.urihttp://hdl.handle.net/11449/34191-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/34191-
dc.description.abstractAntimicrobial peptides (AMPs) are effector molecules of innate immune systems found in different groups of organisms, including microorganisms, plants, insects, amphibians and humans. These peptides exhibit several structural motifs but the most abundant AMPs assume an amphipathic alpha-helical structure. The alpha-helix forming antimicrobial peptides are excellent candidates for protein engineering leading to an optimization of their biological activity and target specificity. Nowadays several approaches are available and this review deals with the use of combinatorial synthesis and directed evolution in order to provide a high-throughput source of antimicrobial peptides analogues with enhanced lytic activity and specificity.en
dc.format.extent473-478-
dc.language.isoeng-
dc.publisherBentham Science Publ Ltd-
dc.sourceWeb of Science-
dc.subjectantimicrobial peptidespt
dc.subjectamphipathic alpha-helixpt
dc.subjectcombinatorial synthesispt
dc.subjectdirected evolutionpt
dc.subjecthigh-throughputpt
dc.titleCombinatorial synthesis and directed evolution applied to the production of alpha-helix forming antimicrobial peptides analoguesen
dc.typeoutro-
dc.contributor.institutionUniversidade de Brasília (UnB)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUniv Brasilia, Dept Cell Biol, Brazilian Ctr Prot Res, BR-70910900 Brasilia, DF, Brazil-
dc.description.affiliationUniv São Paulo, UNESP, Dept Biochem & Chem Technol, Inst Chem, BR-14800900 Araraquara, SP, Brazil-
dc.description.affiliationUnespUniv São Paulo, UNESP, Dept Biochem & Chem Technol, Inst Chem, BR-14800900 Araraquara, SP, Brazil-
dc.identifier.doi10.2174/138920306779025648-
dc.identifier.wosWOS:000241488500002-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofCurrent Protein & Peptide Science-
dc.identifier.orcid0000-0002-4767-0904pt
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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