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
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