Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and Byung Jo Chae

Volume 15, Issue 2, 2008

Page: [188 - 192] Pages: 5

DOI: 10.2174/092986608783489544

Price: $65

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


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy