dbacp06228
General Description
Peptide name : Temporin A
Source/Organism : European common frog
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : FLPLIGRVLSGIL
Peptide length: 13
C-terminal modification: Linear
N-terminal modification : Amidation
Non-natural peptide information: None
Activity Information
Assay type : MTT/MTS assay
Assay time : 6h
Activity : 15% cytotoxicity at 0.5 µg/ml
Cell line : U-937
Cancer type : Lymphoma cancer
Other activity : Anti-bacterial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1397.7465 Dalton
Aliphatic index : 2.023
Instability index : 32.3308
Hydrophobicity (GRAVY) : 1.8077
Isoelectric point : 9.75
Charge (pH 7) : 0.7601
Aromaticity : 0.076
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 5.5
hydrophobic moment : 1.4779
Missing amino acid : C,W,H,Q,T,M,E,K,D,Y,N,A
Most occurring amino acid : L
Most occurring amino acid frequency : 4
Least occurring amino acid : F
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.6)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[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@@H](C)CC)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | ECCEEEEEEEEEE |
| Chou-Fasman (CF) | CEEEEEEEEECCC |
| Neural Network (NN) | CCCCCCCHCCCCE |
| Joint/Consensus | CCCEEEEEEECCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
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
Literature
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.