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Cecropin family
Symbol Cecropin
Pfam PF00272
InterPro IPR000875
SCOP 1f0d
TCDB 1.C.17
OPM superfamily 160
OPM protein 1d9j

Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, from whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.

Cecropins[3][4][5] constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 31 - 37 amino acid residues active against both Gram-positive and Gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names; bactericidin, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related. Cecropin P1, an intestinal antibacterial peptide from Sus scrofa (Pig), also belongs to this family. Cecropin family also consists Cecropin A and Cecropin B.

Cecropin is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.[6] At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.[7]


  1. ^ Cecropins at the US National Library of Medicine Medical Subject Headings (MeSH)
  2. ^ Lauwers A, Twyffels L, Soin R, Wauquier C, Kruys V, Gueydan C (January 2009), "Post-transcriptional regulation of genes encoding anti-microbial peptides in Drosophila", J. Biol. Chem. 284 (13): 8973–83, doi:10.1074/jbc.M806778200, PMC 2659254, PMID 19176529. 
  3. ^ Boman HG, Hultmark D (1987), "Cell-free immunity in insects", Annu. Rev. Microbiol. 41: 103–126, doi:10.1146/annurev.mi.41.100187.000535, PMID 3318666. 
  4. ^ Boman HG (1991), "Antibacterial peptides: key components needed in immunity", Cell 65 (2): 205–207, doi:10.1016/0092-8674(91)90154-Q, PMID 2015623. 
  5. ^ Boman HG, Faye I, Lee JY, Gudmundsson GH, Lidholm DA (1991), "Cell-free immunity in Cecropia. A model system for antibacterial proteins", Eur. J. Biochem. 201 (1): 23–31, doi:10.1111/j.1432-1033.1991.tb16252.x, PMID 1915368. 
  6. ^ Protein Data Bank (1930), Solution structure of CB1a, a novel anticancer peptide derived from natural antimicrobial peptide cecropin B  [<http://www.rcsb.org/pdb/explore/explore.do?structureId=2IGR> <Protein Data Bank>]
  7. ^ Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567