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Cecropin A
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 […]
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.
