Cecropin

Cecropin is a positively charged antimicrobial peptide that is 31-37 amino acids in length. Since they were first isolated from the hemolymph of Hyalophora cecropia, they are called cecropins. Cecropin can not only lyse bacterial cell membranes, but also inhibit proline absorption and cause membrane leakage.

Gram-positive and Gram-negative bacteria are actively againsted by cecropins, which are a major part of the innate immune system of insects. Names for cecropins that have been isolated from insects other than the Hyalophora cecropia (Cecropia moth) include sarcotoxin, lepidopterin, and bactericidin. All of these peptides share structural related. The main members of cecropin include: cecropin A, cecropin B, CECD, Papiliocin and Cecropin P1. Studies have shown that cecropin A can selectively lyse leukemia cells while having little effect on normal lymphocytes. The anticancer activity of cecropin B and cecropin P1 was demonstrated through in vitro studies in mammalian leukemia and lymphoma cell lines.