Cecropin A is an antibacterial peptide originally identified in moths.
Cecropin A has been used as an antimicrobial peptide (AMP):
- to test its cytotoxic effect on breast adenocarcinoma (MDA-MB-231) and human mesothelioma (M14K) cell lines
- in ultrasensitive radial diffusion assay against E coli to test Galleria mellonella protein 24 and apolipophorin III effects
- to test its minimal inhibitory concentrations (MICs) in sensitivity assay for Photorhabdus variants
Cecropin A belongs to cecropin class and comprises 37 amino acid residues in L configuration. Structurally, this peptide has a C-terminal hydrophobic α-helical structure and the amphipathic N-terminal end. Cecropin A is linear and cationic in nature.
Cecropin A interacts with cell membranes and makes it permeable for electrolytes. Cecropin A thus, favors cytolysis and finally cell death in the hepatocellular carcinoma and lymphoma. The synthetic cecropin A in transgenic rice confers protection against bacterial as well as fungal pathogens.