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.
We investigated the in vitro antibiotic activity of the 19-amino acid antimicrobial peptide HP (2-20), derived from the N-terminus of Helicobacter pylori Ribosomal Protein L1 (RPL1), against antibiotic susceptible and resistant pathogens from a patient with gallstones.