Decoralin, a novel linear cationic α-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus
0301 basic medicine
1303 Biochemistry
antimicrobial and leishmanicidal
Wasps
2804 Cellular and Molecular Neuroscience
amphipathic alpha-helix structure
Wasp Venoms
Cationic linear α-helical peptide
In Vitro Techniques
Hemolysis
solitary wasp venom
Cell Degranulation
Protein Structure, Secondary
Antimicrobial and leishmanicidal activity
Mice
03 medical and health sciences
Animals
Humans
Solitary wasp venom
Amino Acid Sequence
Mast Cells
decoralin
Bacteria
activity
Circular Dichroism
1314 Physiology
540
1310 Endocrinology
cationic linear alpha-helical peptide
Rats
Decoralin
Amphipathic α-helix structure
Oligopeptides
Antimicrobial Cationic Peptides
DOI:
10.1016/j.peptides.2007.09.017
Publication Date:
2007-10-02T07:31:00Z
AUTHORS (13)
ABSTRACT
A novel peptide, decoralin, was isolated from the venom of the solitary eumenine wasp Oreumenes decoratus. Its sequence, Ser-Leu-Leu-Ser-Leu-Ile-Arg-Lys-Leu-Ile-Thr, was determined by Edman degradation and corroborated by solid-phase synthesis. This sequence has the characteristic features of linear cationic alpha-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic alpha-helix secondary structure. In fact, the CD spectra of decoralin in the presence of TFE or SDS showed a high alpha-helical conformation content. In a biological evaluation, decoralin exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. A synthetic analog with C-terminal amidation showed a much more potent activity in all the biological assays.
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