cecropins

ce·cro·pins

(sē'krō-pinz),
Antibacterial basic polypeptide consisting of two amphipathic α-helix components, originally isolated from the cecropia moth.

ce·cro·pins

(sē'krō-pinz)
Antibacterial peptides consisting of two amphipathic α-helix components.
References in periodicals archive ?
Activation of both pathways is also important for the entry of AMPs to nucleus such as defensins, cecropins, attacin, and gambicin, which have antiplasmodial activity [14].
In the silkworm, the AMPs have been identified into six groups: cecropins [13-15], moricins [16], gloverins [17], attacins [18], enbocins [19], and lebocins [20, 21].
By consensus, known lepidopteran antimicrobial peptides are arranged into the families of defensins, cecropins and moricins, attacins, gloverins, and lebocins (Rayaprolu et al.
Several inducible AMPs including cecropins, sarcotoxins, defensins, thanatin, droscosin and coleoptericins had been well characterized in terms of the structures and mechanisms [20,21,22,23].
Among AMPs, cecropins (Cec) are small (~4 kDa) peptides containing 35 to 39 amino acids, which are amphipathic, as a high proportion of basic amino acids are present at the N-terminus conferring a net positive charge and the hydrophobic amino acids are rich at the C-terminus (Sipos et al., 1992).
Several antimicrobial peptides produced by epithelial cells are widespread in animal kingdom ranging from Cecropins in insects to Magainins in frogs and Bactenecins in cattle [9-11].
Andreu and colleagues (31), during study on cecropins suggested that AMPs containing more tryptophan are being active against microorganisms.
Zasloff suspects that magainins may be the vertebrate counterpart of cecropins, 37-amino-acid-long antibacterial peptides found circulating in insects such as the Cecropia moth, which lacks both lymphocytes and antibodies.
Kato, "Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum," The Biochemical Journal, vol.
The four groups include Group 1, which consists of linear, cationic, and amphipathic-helical peptides, for example, cecropins, magainins, bombinins, and temporins; Group 2, which consists of [beta]-strands connected by intramolecular disulfide bridges, for example, human [beta]-defensin-2, tachyplesins, and protegrins; Group 3, which consists of linear peptides with an extended structure, characterized by overrepresentation of one or more amino acids, for example, tritrpticin and indolicidin; and Group 4, which consists of peptides containing a looped structure, for example, bactenecin, brevinins, and esculentin.
The selected AMPs with tumoricidal properties are listed in Table 4.AMPssuchasmagainins [111], defensins [112], BMAP-27 and BMAP-28 [113], gaegurins [114], tachyplesin I[115], cecropins, and melittin [99]were reported to exhibit tumoricidal activity against melanoma and carcinoma cells both under in vitro and in vivo conditions.