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- Title
Importance of the length of the N- and C-terminal regions of Helicobacter pylori ribosomal protein L1 (RPL1) on its antimicrobial activity.
- Authors
Park, Yoonkyung; Lee, Dong Gun; Kim, Hee Nam; Kim, Hyung Keun; Woo, Eun-Rhan; Choi, Cheol-Hee; Hahm, Kyung-Soo
- Abstract
HP (2-20) (AKKVFKRLEKLFSKIQNDK-NH2) is an antibacterial 19-mer peptide derived from the N-terminal region of Helicobacter pylori ribosomal protein L1 (RPL1). Several truncated peptides were synthesized to investigate the effects of the N- or C-terminal regions of HP (2-20) on antimicrobial activity. The antimicrobial activity of the peptides was measured by their growth inhibitory effect upon Pseudomonas aeruginosa, Salmonella typhimurium, Saccharomyces cerevisae, Trichosporon beigelii and Candida albicans. Antimicrobial activity required a full length N-terminus. None of the peptides exhibited hemolytic activity against human erythrocyte cells. The membrane-disrupting activity of these peptides, using liposomes and 1,6-diphenyl-1,3,5-hexatriene (DPH) as a probe, confirmed that the full N-terminal region of HP (2-20) is a prerequisite for antibiotic activity and that this region may facilitate penetration of the cell membrane. Circular dichroism indicated that the α-helical structure of the peptides important for antimicrobial activity.
- Subjects
HELICOBACTER pylori; PEPTIDES; PROTEINS; SALMONELLA; PSEUDOMONAS aeruginosa; ENTEROBACTERIACEAE; CANDIDIASIS
- Publication
Biotechnology Letters, 2002, Vol 24, Issue 14, p1209
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1023/A:1016115432642