Antimicrobially active cycloundecapeptides related to gramicidin S having a novel turn structure with cis D-Phe-Pro peptide bond.
Antimicrobially active cycloundecapeptides related to gramicidin S, cyclo(-Val1-Orn2-Leu3-X4-D-Phe5-Pro6-Val7-Orn8- Leu9-D-Phe10-Pro11-) (X= Leu (1), Ala (2), Orn (3), Lys (4) and Arg (5)), were synthesized. From the CD and NMR studies, 1-5 possess antiparallel -sheet conformation linked by a type II -turn around D-Phe10-Pro11 and a novel turn structure around X4-D-Phe5-Pro6 sequence with cis D-Phe-Pro peptide bond. The structural modifications at position 4 of 1-5 are beneficial to identification of novel antibiotic candidates without hemolytic activity.
Tamaki
Makoto
M
Department of Chemistry, Toho University, Funabashi, Chiba 274-8510, Japan. tamaki@chem.sci.toho-u.ac.jp
Sasaki
Ichiro
I
Kokuno
Manabu
M
Shindo
Mitsuno
M
Kimura
Masahiro
M
Uchida
Yoshiki
Y
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects*; D006096:Gramicidin / Q000031:analogs & derivatives*; D008826:Microbial Sensitivity Tests; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D017433:Protein Structure, Secondary
D000900:Anti-Bacterial Agents; D010456:Peptides, Cyclic; D006096:Gramicidin