PMID:15717129
| Citation |
Park, Y and Hahm, KS (2005) 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. 27:193-9 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1007/s10529-004-7875-4 |
| Keywords |
Amino Acid Sequence; Anti-Infective Agents/pharmacology; Bacteria/drug effects; Bacterial Proteins/chemistry; Bacterial Proteins/pharmacology; Candida albicans/drug effects; Candida albicans/ultrastructure; Circular Dichroism; Flow Cytometry; Helicobacter pylori/chemistry; Hemolysis/drug effects; Humans; Microscopy, Confocal; Microscopy, Electron, Scanning; Molecular Sequence Data; Molecular Weight; Peptide Fragments/chemistry; Peptide Fragments/pharmacology; Ribosomal Proteins/chemistry; Ribosomal Proteins/pharmacology; Sequence Analysis, Protein; Sodium Azide/pharmacology; Sodium Chloride/pharmacology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
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