Peptide name : Temporin-1Oc

Source/Organism : Montane brown frog, Asia

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

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 : 1523.8581 Dalton

Aliphatic index : 1.576

Instability index : 38.8615

Hydrophobicity (GRAVY) : 1.6538

Isoelectric point : 9.75

Charge (pH 7) : 0.7601

Aromaticity : 0.230

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

Hydrophobic/hydrophilic ratio : 3.33333333

hydrophobic moment : 1.0556

Missing amino acid : C,W,H,Q,T,M,I,E,K,D,Y,N,V,G

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.6)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)O

1 : Kim JB, et al. Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris. J Pept Res. 2001; 58:349-56. doi: 10.1034/j.1399-3011.2001.00947.x

Paper title : Antimicrobial peptides from the skin of the Japanese mountain brown frog, Rana ornativentris.

Doi : https://doi.org/10.1034/j.1399-3011.2001.00947.x

Abstract : Six peptides with antimicrobial activity were isolated from an extract of freeze-dried skin of the Japanese mountain brown frog Rana ornativentris. Two structurally related peptides (brevinin-20a GLFNVFKGALKTAGKHVAGSLLNQLKCKVSGGC, 11 nmol/g dried tissue, and brevinin-20b GIFNVFKGALKTAGKHVAGSLLNQLKCKVSGEC, 170 nmol/g) belong to the brevinin-2 family, previously identified in Asian and European, but not North American, Ranid frogs. Four peptides (temporin-10a FLPLLASLFSRLL.NH2, 13 nmol/g; temporin-10b FLPLIGKILGTI L.NH2, 350 nmol/g; temporin-10c FLPLLASLFSRLF.NH2, 14 nmol/g; and temporin-10d FLPLLASLFSGLF.NH2, 8 nmol/g) are members of the temporin family first identified in the European common frog Rana temporaria but also found in the skins of North American Ranids. The brevinin-2 peptides showed broad-spectrum activity against the gram-positive bacterium, Staphylococcus aureus, the gram-negative bacterium, Escherichia coli and the yeast Candida albicans, whereas the temporins showed potent activity only against S. aureus. The brevinins and temporins belong to the class of cationic antimicrobial peptides that adopt an amphipathic alpha-helical conformation but it is significant that temporin-10d, which lacks a basic amino acid residue, is still active against S. aureus (minimum inhibitory concentration=13 microM compared with 2 microM for temporin-10a). This suggests that strong electrostatic interaction between the peptide and the negatively charged phospholipids of the cell membrane is not an absolute prerequisite for antimicrobial activity.