Peptide name : Melittin-like peptide (MLP; Frogs, amphibians, animals)

Source/Organism : European common frog

Linear/Cyclic : linear

Chirality : Not found

Peptide length: 22

C-terminal modification: linear

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 : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 2312.7903 Dalton

Aliphatic index : 1.504

Instability index : 21.0545

Hydrophobicity (GRAVY) : 1.2091

Isoelectric point : 10.002

Charge (pH 7) : 1.7581

Aromaticity : 0.090

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 2.66666666

hydrophobic moment : 0.2971

Missing amino acid : C,R,H,T,M,E,D,Y,N

Most occurring amino acid : V

Most occurring amino acid frequency : 4

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.2, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(C)C)C(C)C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)O)C(C)C)C(C)C

1 : Simmaco M, et al. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur J Biochem. 1996; 242:788-92. doi: 10.1111/j.1432-1033.1996.0788r.x

Paper title : Temporins, antimicrobial peptides from the European red frog Rana temporaria.

Doi : https://doi.org/10.1111/j.1432-1033.1996.0788r.x

Abstract : A cDNA library from the skin of Rana temporaria has been screened using a cDNA fragment probe that encodes the signal peptide of the precursor of esculentin from the skin secretion of Rana esculenta. With this approach, the cDNAs encoding the precursors of three peptides were isolated. Subsequently, the peptides predicted from the sequence of the cloned cDNAs as well as several structurally related peptides could be isolated from the skin secretion of R. temporaria. These peptides, which were named temporins, have a length of 10-13 residues and show some sequence similarity to hemolytic peptides isolated from Vespa venom [Argiolas, A. & Pisano, J. J. (1984) J. Biol. Chem. 259, 10106-10111]. Natural and synthetic temporins have antibacterial activity against gram-positive bacteria, but they are not hemolytic. Temporins are the smallest antibacterial peptides hitherto found in nature.