dc.contributor | Universidade de Brasília (UnB) | |
dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.date.accessioned | 2014-05-20T15:23:24Z | |
dc.date.available | 2014-05-20T15:23:24Z | |
dc.date.created | 2014-05-20T15:23:24Z | |
dc.date.issued | 2006-12-01 | |
dc.identifier | Current Protein & Peptide Science. Sharjah: Bentham Science Publ Ltd, v. 7, n. 6, p. 473-478, 2006. | |
dc.identifier | 1389-2037 | |
dc.identifier | http://hdl.handle.net/11449/34191 | |
dc.identifier | 10.2174/138920306779025648 | |
dc.identifier | WOS:000241488500002 | |
dc.identifier | 9424346762460416 | |
dc.identifier | 0000-0002-4767-0904 | |
dc.description.abstract | Antimicrobial 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.language | eng | |
dc.publisher | Bentham Science Publ Ltd | |
dc.relation | Current Protein & Peptide Science | |
dc.relation | 2.696 | |
dc.relation | 0,858 | |
dc.rights | Acesso restrito | |
dc.source | Web of Science | |
dc.subject | antimicrobial peptides | |
dc.subject | amphipathic alpha-helix | |
dc.subject | combinatorial synthesis | |
dc.subject | directed evolution | |
dc.subject | high-throughput | |
dc.title | Combinatorial synthesis and directed evolution applied to the production of alpha-helix forming antimicrobial peptides analogues | |
dc.type | Otros | |