title: Antibacterial peptides designed as analogs or hybrids of cecropins and melittin.
abstract: Eight new analogs of cecropin A, two new analogs of melittin and 30 hybrid peptides containing sequences from cecropins and melittin have been synthesized. The lengths of the peptides have varied from 37 residues (the length of cecropin A) to 18 residues. The peptides have been assayed for lysis of sheep red blood cells and for antibacterial activity against two Gram negative and three Gram positive bacteria. The best analogs of cecropin A maintained the anti-Escherichia coli activity of the parental peptide, and were not lytic for red blood cells. Melittin and its replacement analogs were all lytic for red blood cells, but an analog with transposed segments was not. Several of the hybrid peptides were found to be both non-hemolytic and highly active against all test bacteria. The data were used to define the structural requirements for antibacterial activity.
authors: Rockefeller University, New York, NY.
authors: D
authors: D
authors: Wade
authors: D
authors: D
authors: Andreu
authors: S A
authors: SA
authors: Mitchell
authors: A M
authors: AM
authors: Silveira
authors: A
authors: A
authors: Boman
authors: H G
authors: HG
authors: Boman
authors: R B
authors: RB
authors: Merrifield
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D001419:Bacteria / Q000187:drug effects; D007301:Insect Hormones / Q000737:chemistry* / Q000494:pharmacology; D008555:Melitten / Q000031:analogs & derivatives* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D007301:Insect Hormones; D010446:Peptide Fragments; D010455:Peptides; D008555:Melitten; C031161:cecropin A