Structure and Antibiotic Activity of a Porcine Myeloid Antibacterial Peptide, PMAP-23 and its Analogues

  • Shin, Song-Yub (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kang, Joo-Hyun (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology) ;
  • Jang, So-Yun (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Kil-Lyong (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology) ;
  • Hahm, Kyung-Soo (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology)
  • 투고 : 1999.07.31
  • 심사 : 1999.09.17
  • 발행 : 2000.01.31

초록

PMAP-23 is a 23-residue antimicrobial peptide derived from porcine myloid cells. In order to investigate the effects of two Pro residues at positions 12 and 15 of PMAP-23 on antibiotic activity, two analogues in which Ala was substituted for Pro residue at position 12 or 15 were synthesized. $Pro^{12}{\rightarrow}Ala$ (PMAPl) or $Pro^{15}{\rightarrow}Ala$(PMAP2) substitution in PMAP-23 caused a significant reduction on antitumor and phospholipid vesicle-disrupting activities, but did not cause a significant effect on antibacterial activity. PMAP-23 displayed the type I ${\beta}-turn$ structure with a negative ellipticity at near 205 om in SDS micelle, whereas PMAP1 and PMAP2 had a somewhat ${\alpha}-helical$ propensity in TFE solution, as compared to PMAP-23. These results suggest that two Pro residues of positions 12 and 15 in PMAP-23 play important roles in the formation of ${\beta}-turn$ structure on lipid membrane and its ${\beta}-turn$ structure may be essential for antibiotic activity including phospholipid vesicle-disrupting property.

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