Cecropin

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]

References

↑ Cecropins at the US National Library of Medicine Medical Subject Headings (MeSH)
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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>]
↑ Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567

v t e Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin	SAG ARRB1 ARRB2 ARR3

Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18

Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero

Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C

Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34

Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF

see also other cell membrane protein disorders B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), other

v t e Pore-forming toxins (TC 1C)

Antimicrobial cationic peptides	Cathelicidin Defensin Dermcidin Histatin (HTN1, HTN3)

Other, human	Perforin

Other, nonhuman	Cecropin Diphtheria toxin Dermaseptin Magainin Melittin Nisin Pneumolysin

B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), other

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