Cecropins are small proteins anywhere from 31 - 37 amino acids long and are active against both gram-positive and gram-negative bacteria.

[12] Cecropins from many insect species have been shown to be active against a diverse range of human cancer cell lines.

[13] Flow cytometry and RT-PCR experiments revealed that treatment with Mdcec increased expression of pro-apoptotic genes such as caspase-3, leading to cancer cell death.

[14] In the same study, chemotherapy drugs cytarabine and 5-fluorouracil synergize with cecropin A in vitro to enhance cytotoxic effects on leukemia cells.

[14] This indicates potential for therapeutic application of antimicrobial peptides in cancer, where treatment with cecropins could lower the required dosage of chemotherapy drugs, reducing undesirable side effects.

[6][15] Repeated administration of peptides is necessary to maintain systemic levels of cecropins at sufficient concentrations for anti-cancer activity.

Cecropin A can destroy planktonic and sessile biofilm-forming uropathogenic E. coli (UPEC) cells, either alone or when combined with the antibiotic nalidixic acid, synergistically clearing infection in vivo (in the insect host Galleria mellonella) without off-target cytotoxicity.

The multi-target mechanism of action involves outer membrane permeabilization followed by biofilm disruption triggered by the inhibition of efflux pump activity and interactions with extracellular and intracellular nucleic acids.