Peptide name : temporin-PEa

Source/Organism : Synthetic analog of Temporin-PE

Linear/Cyclic : Linear

Chirality : L

Peptide length: 13

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : Not Available

Activity : IC50 = 3.520 μM

Cell line : U251-MG

Cancer type : Brain Tumor

Other activity : Antimicrobial and Anticancer

Amino acid composition bar chart :

Molecular mass : 1449.8177 Dalton

Aliphatic index : 2.1

Instability index : -3.8308

Hydrophobicity (GRAVY) : 1.9923

Isoelectric point : 8.5909

Charge (pH 7) : 0.7581

Aromaticity : 15.38

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

Hydrophobic/hydrophilic ratio : 3.3333

hydrophobic moment : 1.2333

Missing amino acid : C,D,E,H,M,N,P,Q,R,T,W

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (53., 15., 69.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O)C(C)C

1 : Sang M, et al. Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus. Biochem Biophys Res Commun. 2018; 495:2539-2546. doi: 10.1016/j.bbrc.2017.11.173

Paper title : Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus.

Doi : https://doi.org/10.1016/j.bbrc.2017.11.173

Abstract : A potent natural antimicrobial peptide named temporin-PE was identified and encoded from the skin secretions of Pelophylax kl. esculentus via "shotgun" cloning and LC-MS/MS fragmentation analysis. Target-modifications were carried out to further enhance the antimicrobial and anti-proliferative bioactivities, whilst decreasing the hemolytic effect. A range of bioassays demonstrated that replacing a proline with a tyrosine residue resulted in a loss of the bioactivity against Gram-negative bacteria, but dramatically improved the hemolytic and anti-proliferative activity, indicating the FLP- motif influences the hemolytic activity of temporins. Moreover, the coupling of TAT to the peptide dramatically improved its antimicrobial activity, indicating coupling TAT to these peptides could be considered as a potential tool to improve their antimicrobial activity. Overall, we have shown that targeted modifications of this natural antimicrobial peptide can adjust its bioactivities to help its development as an antibiotic or anti-proliferative agent.