Peptide name : Decoralin

Source/Organism : Venom, solitary eumenine wasp

Linear/Cyclic : Linear

Chirality : L

Peptide length: 11

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Amino acid composition bar chart :

Molecular mass : 1256.5774 Dalton

Aliphatic index : 2.127

Instability index : 1.3727

Hydrophobicity (GRAVY) : 1.2273

Isoelectric point : 11.000

Charge (pH 7) : 1.4591

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 1.2

hydrophobic moment : -1.031

Missing amino acid : C,W,H,Q,P,M,E,F,D,Y,N,A,V,G

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : R

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.1, 0.6)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@H](C(=O)O)[C@@H](C)O)[C@@H](C)CC

1 : Konno K, et al. Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus. Peptides. 2007; 28:2320-7. doi: 10.1016/j.peptides.2007.09.017

Paper title : Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus.

Doi : https://doi.org/10.1016/j.peptides.2007.09.017

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.