Abstract
HP (2-20) [derived from the N-terminal region of Helicobacter pylori Ribosomal Protein L1 (RPL1)], a 19-mer peptide, possesses broad-spectrum anti-microbial activity. As the N- (residues 2–3) and C-terminal (residues 14–20) residues can be deleted without affecting antimicrobial activity, we have now determined the minimum chain length necessary for the retention of antimicrobial activity, and its mode of action. The N- (residues 2–3) and C-terminal (residues 17–20) truncated fragments [HP (4–16)] induce increased antibiotic activity against several bacterial strains without hemolysis. Flow cytometric analysis, scanning electron microscopy and fluorescence confocal microscopy revealed that HP (4–16) acted rapidly on the plasma membranes of the fungal cells in a salt- and energy-independent manner.
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Revisions requested 16 September 2004/1 November 2004; Revisions received 29 October 2004/8 December 2004
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Park, Y., Hahm, KS. Effects of N- and C-terminal truncation of HP (2-20) from Helicobacter pylori ribosomal protein L1 (RPL1) on its anti-microbial activity. Biotechnol Lett 27, 193–199 (2005). https://doi.org/10.1007/s10529-004-7875-4
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DOI: https://doi.org/10.1007/s10529-004-7875-4