Cecropin

Cecropin family

2IGR ?
Identifiers
Symbol Cecropin
Pfam PF00272
InterPro IPR000875
PROSITE PDOC00241
SCOP 1f0d
SUPERFAMILY 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, 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, lepidopterin, sarcotoxin, etc. All of these peptides are structurally related.

Members

Members include :

Cecropin A
Peptide Sequence (KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK). Secondary structure includes two α helices.[6]:4.2 At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.[7]
Cecropin B
Peptide Sequence (KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL). Secondary structure includes two α helices.[6]:4.2
CECD
from Aedes aegypti (Yellowfever mosquito).[8]
Papiliocin
(A lepidopteran) from Papilio xuthus[8] an Asian swallowtail butterfly.
Cecropin P1
An antibacterial peptide from Ascaris suum, a parasitic nematode that resides in the pig intestine, also belongs to this family.

Derivatives

A derivative of Cecropin B is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.[9]

Some of the cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called anticancer peptides (ACPs).[6]:3 Hybrid ACPs based on Cecropin A have been studied for anticancer properties.[6]:7.1

References

  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. 1 2 3 4 Hoskin, D.W.; Ramamoorthy, A. (February 2008), "Studies on anticancer activities of antimicrobial peptides", Biochimica et Biophysica Acta (BBA) - Biomembranes 1778 (2): 357–375, doi:10.1016/j.bbamem.2007.11.008, PMC 2238813, PMID 18078805
  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
  8. 1 2 cecropin family OPM
  9. ↑ 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>]

Further reading

External links


This article is issued from Wikipedia - version of the Sunday, February 14, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.