Antibiotic Activity of Antimicrobial Peptide Against Pseudomonads Isolated from a Patient with Gallstones
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. HP (2-20) was active against antibiotic-susceptible and antibiotic-resistant clinical isolates of pathogens from a patient with gallstones, but this peptide showed no hemolytic activity against normal human erythrocytes. HP (2-20) acted synergistically with ciprofloxacin against pathogenic bacteria. Fluorescence activated flow cytometry revealed that the effect of HP (2-20) was dependent on energy and salt concentration. In addition, scanning electron microscopy showed that HP (2-20) caused significant morphological alterations to the cell surface of pathogens. Using 16S rDNA sequences, we found that isolates from bile were 100% homologous to Pseudomonas aeruginosa. These findings suggest that HP (2-20) may be useful clinically as an antibiotic against acquired pathogens from patients with gallstones and against pathogens resistant to other antibiotics.
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Document Type: Research Article
Affiliations: Research Center for Proteineous Materials (RCPM), Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, Korea.
Publication date: 2006-01-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.