Cecropin
From Wikipedia, the free encyclopedia
Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.
| Cecropin family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Model of Drosophila melanogaster Cecropin A | |||||||||
| Identifiers | |||||||||
| Symbol | Cecropin | ||||||||
| Pfam | PF00272 | ||||||||
| InterPro | IPR000875 | ||||||||
| PROSITE | PDOC00241 | ||||||||
| SCOP2 | 1f0d / SCOPe / SUPFAM | ||||||||
| TCDB | 1.C.17 | ||||||||
| OPM superfamily | 151 | ||||||||
| OPM protein | 1d9j | ||||||||
| |||||||||
Cecropins[3][4][5] constitute a main part of the innate immune system of insects. Cecropins are small proteins anywhere from 31 - 37 amino acids long and are active against both gram-positive and gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names, such as bactericidin, lepidopterin, and sarcotoxin. All of these peptides are structurally related.