Cecropin A – Potent antimicrobial and anticancer peptide
Cecropin A is an antimicrobial peptide active against Gram-positive and Gram-negative bacteria. Some studies have suggested that cecropin A binds to negatively charged membrane lipids and form a packed layer which permeabilize the membranes and help to kill bacteria. It was shown that cecropin A presents a LC50 of 0.9 µM and a LC90 of 1.7 µM against certain E.Coli strains. Besides its well-known antimicrobial properties, studies have demonstrated tumoricidal activity of cecropin A against leukemia, lymphoma, colon carcinoma cell lines and other tumour cell lines. Furthermore, Cecropin A has a fungicidal activity. A study has shown that cecropin A reaches a complete lethality at approximately 25 mM for germinating conidia of Aspergillus spp. and a complete lethality for nongerminated and germinated conidia of Fusarium spp. at 1.5 mM.
BACKGROUND: Cecropin A is a novel 37-residue cecropin-like antimicrobial peptide isolated from the cecropia moth, Hyalophora cecropia. We have demonstrated that cecropin A is an antibacterial agent and have investigated its mode of action. In this study, we show that cecropin A has potent antimicrobial activity against 2 multidrug resistant organisms-Acinetobacter baumanii and-Pseudomonas aeruginosa.
METHOD/RESULTS: Interactions between cecropin A and membrane phospholipids were studied using tryptophan blue shift experiments. Cecropin A has a strong interaction with bacterial cell mimetic membranes. These results imply that cecropin A has selectivity for bacterial cells. To address the potential the rapeutic efficacy of cecropin A, its anti-inflammatory activities and mode of action in mouse macrophage-derived RAW264.7 cells stimulated with lipopolysaccharide (LPS) were examined. Cecropin A suppressed nitrite production, mTNF-α, mIL-1β, mMIP-1, and mMIP-2 cytokine release in LPS-stimulated RAW264.7 cells. Furthermore, cecropin A inhibited intracellular cell signaling via the ERK, JNK, and p38 MAPK pathway, leading to the prevention of COX-2 expression in LPS-stimulated RAW264.7 cells.
CONCLUSION: These results strongly suggest that cecropin A should be investigated as a potential agent for the prevention and treatment of inflammatory diseases.
2- Silvestro, L et al. Antimicrobial agents and chemotherapy vol. 44,3 (2000)
BACKGROUND: The ability of cecropin A to permeabilize and depolarize the membranes of Escherichia coli ML-35p bacteria has been compared to its bactericidal activity in an extension of earlier studies performed on synthetic lipid vesicle membranes (L. Silvestro, K. Gupta, J. H. Weiser, and P. H. Axelsen, Biochemistry 36:11452–11460, 1997).
OBJECTIVE: Ability of cecropin A to permeabilize and depolarize the membranes of Escherichia coli
METHOD/RESULTS: Our results indicate that differences in the concentration dependences of membrane permeabilization and depolarization seen in synthetic vesicles are not manifested in whole bacteria.
CONCLUSION: The concentration dependences of both phenomena roughly correlate with bactericidal activity, suggesting that the bactericidal mechanism of cecropin A is related to membrane permeabilization.
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