N-terminal analogues of cecropin A: synthesis, antibacterial activity, and conformational properties.
Six analogues of the 37-residue antibacterial peptide cecropin A were synthesized by the solid-phase method: cecropin A-(2-37), [Glu2]cecropin A, [Pro4]cecropin A, [Glu6]cecropin A, [Leu6]cecropin A, and [Pro8]cecropin A. Their antibacterial activities against four test organisms were determined and related to conformational changes observed in their CD spectra and were discussed on the basis of a previously proposed amphipathic alpha-helix model. An aromatic residue in position 2 was shown to be important for activity against all tested bacteria. The highly alpha-helical 1-11 region of cecropin A did not appear to play a significant role in its activity against Escherichia coli but was clearly involved in its interaction against Pseudomonas aeruginosa, Bacillus megaterium, and Micrococcus luteus.
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D001410:Bacillus megaterium / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D007301:Insect Hormones / Q000138:chemical synthesis* / Q000494:pharmacology; D008837:Micrococcus / Q000187:drug effects; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000138:chemical synthesis*; D011550:Pseudomonas aeruginosa / Q000187:drug effects; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D007301:Insect Hormones; D010446:Peptide Fragments; C031161:cecropin A