Peptide name : Tigerinin 1

Source/Organism : Skin secretions, Indian bullfrog, India, Asia

Linear/Cyclic : Cyclic

Chirality : Not found

Peptide length: 11

C-terminal modification: Cyclic

N-terminal modification : Not found

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 : Not found

Amino acid composition bar chart :

Molecular mass : 1343.6793 Dalton

Aliphatic index : 0.709

Instability index : 26.6364

Hydrophobicity (GRAVY) : 0.8182

Isoelectric point : 8.0582

Charge (pH 7) : 0.7393

Aromaticity : 0.181

Molar extinction coefficient (cysteine, cystine): (1490, 1615)

Hydrophobic/hydrophilic ratio : 2.66666666

hydrophobic moment : 0.126

Missing amino acid : W,H,Q,E,K,S,D,L,N,A,V,G

Most occurring amino acid : C

Most occurring amino acid frequency : 2

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.0, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O)[C@@H](C)CC

1 : Sai KP, et al. Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina. J Biol Chem. 2001; 276:2701-7. doi: 10.1074/jbc.M006615200

Paper title : Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina.

Doi : https://doi.org/10.1074/jbc.M006615200

Abstract : Four broad-spectrum, 11 and 12 residue, novel antimicrobial peptides have been isolated from the adrenaline-stimulated skin secretions of the Indian frog Rana tigerina. Sequences of these peptides have been determined by automated Edman degradation, by mass spectral analysis and confirmed by chemical synthesis. These peptides, which we have named as tigerinins, are characterized by an intramolecular disulfide bridge between two cysteine residues forming a nonapeptide ring. This feature is not found in other amphibian peptides. Conformational analysis indicate that the peptides tend to form beta-turn structures. The peptides are cationic and exert their activity by permeabilizing bacterial membranes. Tigerinins represent the smallest, nonhelical, cationic antimicrobial peptides from amphibians.