Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 7, Issue 6, Pages 473-478Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920306779025648
Keywords
antimicrobial peptides; amphipathic alpha-helix; combinatorial synthesis; directed evolution; high-throughput
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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.
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