dc.contributorUniversidade de Brasília (UnB)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:23:24Z
dc.date.available2014-05-20T15:23:24Z
dc.date.created2014-05-20T15:23:24Z
dc.date.issued2006-12-01
dc.identifierCurrent Protein & Peptide Science. Sharjah: Bentham Science Publ Ltd, v. 7, n. 6, p. 473-478, 2006.
dc.identifier1389-2037
dc.identifierhttp://hdl.handle.net/11449/34191
dc.identifier10.2174/138920306779025648
dc.identifierWOS:000241488500002
dc.identifier9424346762460416
dc.identifier0000-0002-4767-0904
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.
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationCurrent Protein & Peptide Science
dc.relation2.696
dc.relation0,858
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectantimicrobial peptides
dc.subjectamphipathic alpha-helix
dc.subjectcombinatorial synthesis
dc.subjectdirected evolution
dc.subjecthigh-throughput
dc.titleCombinatorial synthesis and directed evolution applied to the production of alpha-helix forming antimicrobial peptides analogues
dc.typeOtros


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