• Title/Summary/Keyword: PMAP-23

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

  • Shin, Song-Yub;Kang, Joo-Hyun;Jang, So-Yun;Kim, Kil-Lyong;Hahm, Kyung-Soo
    • BMB Reports
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    • v.33 no.1
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    • pp.49-53
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    • 2000
  • 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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Structural Studies of Porcine Myeloid Antibacterial Peptide, PMAP-23 in DPC micelles by NMR Spectroscopy

  • Park, Kyoungsoo;Songyub Shin;Kyungsoo Hahm;Kim, Yangmee
    • Proceedings of the Korean Biophysical Society Conference
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    • 2001.06a
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    • pp.29-29
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    • 2001
  • Leukocytes are important elements in the host defense against microbial infections. A variety of antimicrobial peptides named as the cathelicidin family have been identified from leukocytes. PMAP-23 derived from porcine myeloid cells is an antimicrobial peptide belong to the cathelicidin family. PMAP-23 was reported to have potent growth inhibition activity against bacterial and tumor cells with no hemolytic activity.(omitted)

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Interactions of Membrane and PMAP-23 Studied by $^{31}P$ solid-state NMR Spectroscopy

  • Kim, Si-Won;Kim, Suhk-Mann
    • Journal of the Korean Magnetic Resonance Society
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    • v.11 no.2
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    • pp.110-114
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    • 2007
  • [ $^{31}P$ ] powder pattern spectra were measured to investigate the aspects of the interaction between the MLV (Multilamellar vesicle) and PMAP-23, a membrane of cathelicidin family and then CSAs(chemical shift anisotropy) were calculated to indentify the extent of perturbation of phospholipid mobility by the peptides. We found that acidic phospholipid interacts strongly with PMAP-23, and the analogues which modified to increase the amphipathic property showed that larger change of CSA. The analogue which introduced positive charge showed the same effects with amphipathic property.

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