Cecropin A is an antimicrobial peptide originally isolated from insects, but now believed to be naturally produced and found in a large variety of organisms including mammals. It has garnered a lot of interest for its broad-spectrum antiparasitic and antibacterial activities. It is also active against fungi, and has cytotoxic effects on cancer cell lines. It is common to find this peptide as part of a fusion protein or the beginnings of a derived series of antimicrobial peptides in new antimicrobial drug research.
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| Mechanism of Action | The antibacterial mode of action for Cecropins is pore-formation based, in which an antimicrobial peptide inserts itself into the bacterial membrane and allows ions to flow freely through, resulting in cell depolarization and death. |
| Microbiology Applications |
Liu et al have developed the amide-modified antimicrobial peptide (AMP) CecXJ-37N, based on one of many cecropin AMPs, cecropin XJ. It is being designed and tested specifically with the food industry in mind, as an antibacterial food preservative. Microbe contamination can cause serious food-borne illness, but chemical preservatives like nitrites and sulfites can be cause for other safety concerns; CecXJ-37N is derived from a natural product, and will hopefully exemplify a better safety profile. Showing potent antibacterial activity against Gram-positive and Gram-negative bacteria in addition to low cytotoxicity and a negative hemolytic rate, CecXJ-37N shows promise as a safe antibacterial agent for the food industry. Its mechanism of action was also investigated, showing incredibly fast cytolysis in addition to a DNA-based interaction. We look forward to their planned further study on CecXJ-37N’s apparent ability to intercalate into nucleotides of DNA, and the binding’s effect on antibacterial activity and cytotoxicity. Once a new, naturally-occuring antimicrobial is found, it needs to be easy to produce in order for it to be medically useful. Cecropin A is a broad-spectrum antibiotic and antifungal peptide originally isolated from insect haemolymph. In this paper, Montesinos et al. developed a more-abundant production method for this antimicrobial peptide with rice seeds. Since organisms are already creating their own peptides, researchers can "piggy-back" on that process to produce desirable antimicrobial peptides. In this case, the rice seeds were genetically modified with the gene to create Cecropin A fused to an existing rice peptide Ole18. The rice seeds produced this fusion-peptide, and then it was extracted from the seed. The Ole18-CecA fusion protein was separated by proteolytic digestion. It was estimated that 6ug of CecA can be recovered per gram of rice seeds (Montesinos et al, 2016). |
| Molecular Formula | C184H313N53O46 |
| References |
Cerón, J. M., Contreras-Moreno, J., Puertollano, E., Cienfuegos, G. Á, Puertollano, M. A., & Pablo, M. A. (2010). The antimicrobial peptide cecropin A induces caspase-independent cell death in human promyelocytic leukemia cells. Peptides, 31(8), 1494-1503. doi:10.1016/j.peptides.2010.05.008 Dongliang Liu D et al (2017) A potential food biopreservative, CecXJ-37N, non-covalently intercalates into the nucleotides of bacterial genomic DNA beyond membrane attack. Food Chem. 217:576-584 Montesinos et al (2016).Production of biologically active Cecropin A peptide in rice seed oil bodies. Link. |
