Abstract
In a previous study, we reported that truncation of HP (2-20) (derived from the N-terminal region of Helicobacter pylori Ribosomal Protein L1 (RPL1)) at the N- (residues 2-3) and C-terminal (residues 17-20) truncated fragments to give HP (4-16) induces increased antibiotic activity against several bacterial strains without hemolysis. In this study, to develop novel short antibiotic peptides useful as therapeutic drugs, an analogue was designed to possess increased hydrophobicity by Trp substitution in position 2 region of HP (4-16). Synthetic HP (4-16)-W showed an enhanced antimicrobial and antitumor activity. The antimicrobial activity of this peptide and others was measured by their growth inhibitory effect upon S. aureus, B. subtilis, S. epidermidis, E. coli, S. typimurium, P. aeruginosa, C. albicans, T. beigelii and S. cerevisiae. None of the peptides exhibited hemolytic activity against human erythrocyte cells except melittin as a positive control. Its antibiotic activity suggests that HP (4-16)-W is an excellent candidate as a lead compound for the development of novel antibiotic agents.
Keywords: Helicobacter pylori ribosomal protein L1, antimicrobial activity, HP (4-16)-W, hemolytic activity, antibiotic agents, erythrocyte cells, innate immunity, cecropin-like peptide, gastrointestinal illness, peptic ulcers
Protein & Peptide Letters
Title:Novel Short AMP: Design and Activity Study
Volume: 19 Issue: 6
Author(s): Yoonkyung Park and Kyung-Soo Hahm
Affiliation:
Keywords: Helicobacter pylori ribosomal protein L1, antimicrobial activity, HP (4-16)-W, hemolytic activity, antibiotic agents, erythrocyte cells, innate immunity, cecropin-like peptide, gastrointestinal illness, peptic ulcers
Abstract: In a previous study, we reported that truncation of HP (2-20) (derived from the N-terminal region of Helicobacter pylori Ribosomal Protein L1 (RPL1)) at the N- (residues 2-3) and C-terminal (residues 17-20) truncated fragments to give HP (4-16) induces increased antibiotic activity against several bacterial strains without hemolysis. In this study, to develop novel short antibiotic peptides useful as therapeutic drugs, an analogue was designed to possess increased hydrophobicity by Trp substitution in position 2 region of HP (4-16). Synthetic HP (4-16)-W showed an enhanced antimicrobial and antitumor activity. The antimicrobial activity of this peptide and others was measured by their growth inhibitory effect upon S. aureus, B. subtilis, S. epidermidis, E. coli, S. typimurium, P. aeruginosa, C. albicans, T. beigelii and S. cerevisiae. None of the peptides exhibited hemolytic activity against human erythrocyte cells except melittin as a positive control. Its antibiotic activity suggests that HP (4-16)-W is an excellent candidate as a lead compound for the development of novel antibiotic agents.
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Cite this article as:
Park Yoonkyung and Hahm Kyung-Soo, Novel Short AMP: Design and Activity Study, Protein & Peptide Letters 2012; 19 (6) . https://dx.doi.org/10.2174/092986612800494093
DOI https://dx.doi.org/10.2174/092986612800494093 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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