[Synthesis and antibacterial activity of analogues of the N-terminal fragment of the sarcotoxin IA antimicrobial peptide].
Three 18-membered analogues of the N-terminal fragment of the sarcotoxin IA cationic antimicrobial peptide were synthesized by the solid phase method of peptide synthesis with the use of swellographic monitoring. The ability of these peptides to inhibit the growth of various bacteria in culture medium and their hemolytic activity in experiments on human erythrocytes were studied. The analogue completely corresponding to the N-terminal amino acid sequence of the natural sarcotoxin IA with the amide group on its C-terminus exhibited higher antibacterial activity. The presence of carboxyl group on the C-terminus or the substitution of Tyr for Trp2 resulted in a decrease in the antimicrobial activity of the peptide. Our results indicate that the amphiphilic N-terminal peptide corresponding to the 1-18 sequence of sarcotoxin IA involves the moieties responsible for the antimicrobial activity of the antibiotic.
Taran
S A
SA
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry (Pushchino Branch), Russian Academy of Sciences, Pushchino, Moscow Oblast, 142292 Russia. nucleus@fibkh.serpukhov.su
Esikova
T Z
TZ
Mustaeva
L G
LG
Baru
M B
MB
Alakhov
Iu B
IuB
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D001410:Bacillus megaterium / Q000187:drug effects* / Q000254:growth & development; D015169:Colony Count, Microbial; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects* / Q000254:growth & development; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D019476:Insect Proteins / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data
D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; C054733:sarcotoxin IA protein, Sarcophaga peregrina