Biological activities of C-terminal 15-residue synthetic fragment of melittin: design of an analog with improved antibacterial activity.
Melittin, the 26-residue predominant toxic peptide from bee venom, exhibits potent antibacterial activity in addition to its hemolytic activity. The synthetic peptide of 15 residues corresponding to its C-terminal end (MCF), which encompasses its most amphiphilic segment, is now being shown to possess antibacterial activity about 5-7 times less compared to that of melittin. MCF, however, is 300 times less hemolytic. An analog of MCF, MCFA, in which two cationic residues have been transpositioned to the N-terminal region from the C-terminal region, exhibits antibacterial activity comparable to that of melittin, but is only marginally more hemolytic than MCF. The biophysical properties of the peptides, like folding and aggregation, correlate well with their biological properties.
Subbalakshmi
C
C
Centre for Cellular and Molecular Biology, Hyderabad, India.
Nagaraj
R
R
Sitaram
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D001412:Bacillus subtilis / Q000187:drug effects; D001516:Bees; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D006461:Hemolysis; D008555:Melitten / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000187:drug effects; D051381:Rats; D013211:Staphylococcus aureus / Q000187:drug effects
D000900:Anti-Bacterial Agents; D008555:Melitten