Synthesis and antibiotic activities of CRAMP, a cathelin-related antimicrobial peptide and its fragments
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- Synthesis and antibiotic activities of CRAMP, a cathelin-related antimicrobial peptide and its fragments
- Jong Myung Ha; Song Yub Shin; Shin Won Kang
- Bibliographic Citation
- Bulletin of Korean Chemical Society, vol. 20, no. 9, pp. 1073-1077
- Publication Year
- CRAMP, a 37-amino acid cationic antimicrobial peptide was recently deduced from the cDNA cloned from mouse femoral marrow RNA. In order to investigate the structure-activity relationship and functional region of CRAMP, CRAMP and its 18-mer overlapping peptides were synthesized by the solid phase method. CRAMP showed broad spectrum antibacterial activity against both Gram-positive and Gram-negative bacterial strains (MIC: 3.125- 6.25 μM) but had no hemolytic activity until 50 μM. CRAMP was found to have a potent anticancer activity (IC50: 12-23 μM) against two human small cell lung cancer cell lines. Furthermore, CRAMP was found to display faster bactericidal rate in B. subtilis rather than E. coli in the kinetics of bacterial killing. Among 18-meric overlapping fragment peptides, only CRAMP (16-33) displayed potent antibacterial activity (MIC: 12.5-50 μM) against several bacteria with no hemolytic activity. Circular dichroism (CD) spectra analysis indicated that CRAMP and its analogues will form the amphipathic α- helical conformation in the cell membranes similar to other antimicrobial peptides, such as cecropins and magainins.
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