Influence of the N- and C-Terminal Regions of Leu-Lys Rich Antimicrobial Peptide on Antimicrobial Activity

Author(s): Yoonkyung Park, Hae Kyun Park, Hak-Tae Lim, Byung Jo Chae, Kyung-Soo Hahm, Hae Kyun Park, Byung Jo Chae

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 2 , 2008

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Abstract:

P5 (KWKKLLKKPLLKKLLKKL-NH2) 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, K3K4L5L6-deleted peptide, acted independent on the ionic environment. Furthermore, P11 causes significant morphological alterations of the fungal surfaces as shown by scanning electron microscopy.

Keywords: Antimicrobial activity, Leu-Lys rich peptide, P11 peptide, scanning electron microscopy

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Article Details

VOLUME: 15
ISSUE: 2
Year: 2008
Page: [188 - 192]
Pages: 5
DOI: 10.2174/092986608783489544
Price: $65

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