Influence of the N- and C-terminal regions of leu-lys rich antimicrobial peptide on antimicrobial activity.
P5 (KWKKLLKKPLLKKLLKKL-NH(2)) is an antibacterial 18-mer Leu-Lys rich peptide from CA (1-8)-MA (1-12) hybrid peptide (CA-MA). Here we show that decreasing the net hydrophobicity and charge of CA-MA by deleting Leu- or Lys- of the N- or C-terminal regions of P5 (P10 or P11). The antimicrobial activity of the peptides was measured by their growth inhibitory effect upon S. aureus, B. subtilis, P. aeruginosa, S. typhimurium, E. coli, T. beigelii and C. albicans. Antimicrobial activity required a full length C-terminus. Confocal microscopy showed that P11 was located in the plasma membrane. In this study, P11, K(3)K(4)L(5)L(6)-deleted peptide, acted independent on the ionic environment. Furthermore, P11 causes significant morphological alterations of the fungal surfaces as shown by scanning electron microscopy.
Park
Hae Kyun
HK
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Lim
Hak-Tae
HT
Chae
Byung Jo
BJ
Hahm
Kyung-Soo
KS
Park
Yoonkyung
Y
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D002176:Candida albicans / Q000166:cytology / Q000187:drug effects; D007930:Leucine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D012492:Salts / Q000737:chemistry
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D012492:Salts; D007930:Leucine; D008239:Lysine