Peptide name : Tempoprin-1CEa

Source/Organism : Chinese brown frog

Linear/Cyclic : Linear

Chirality : L

Peptide length: 15

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 1h

Activity : 30 % Cell viability at 40 µM

Cell line : Bcap-37

Cancer type : Breast cancer

Other activity : Anti-microbial

Amino acid composition bar chart :

Molecular mass : 1735.0743 Dalton

Aliphatic index : 1.56

Instability index : 17.2867

Hydrophobicity (GRAVY) : 0.9533

Isoelectric point : 8.5909

Charge (pH 7) : 0.7592

Aromaticity : 0.133

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

Hydrophobic/hydrophilic ratio : 1.5

hydrophobic moment : -0.121

Missing amino acid : C,R,W,H,Q,T,P,M,E,Y,G

Most occurring amino acid : I

Most occurring amino acid frequency : 4

Least occurring amino acid : V

Least occurring amino acid frequency : 1

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

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

1 : Wang C, et al. Anticancer mechanisms of temporin-1CEa, an amphipathic α-helical antimicrobial peptide, in Bcap-37 human breast cancer cells. Life Sci. 2013; 92:1004-14. doi: 10.1016/j.lfs.2013.03.016

Paper title : Anticancer mechanisms of temporin-1CEa, an amphipathic α-helical antimicrobial peptide, in Bcap-37 human breast cancer cells.

Doi : https://doi.org/10.1016/j.lfs.2013.03.016

Abstract : AIMS: Temporin-1CEa, a 17-residue antimicrobial peptide, is known to exert broad-spectrum anticancer activity that acts preferentially on cancer cells instead of normal cells. However, the mechanism of cancer cell death induced by temporin-1CEa is weakly understood. MAIN METHODS: Here, we investigated the cytotoxic and membrane-disrupting effects of temporin-1CEa on human breast cancer cell line Bcap-37, using MTT assay, electronic microscope observation, fluorescence imaging and flow cytometry analysis. KEY FINDINGS: The MTT assay indicated that one-hour temporin-1CEa treatment led to rapid cell death in either caspase-dependent or -independent manner. The electronic microscope observation suggested that temporin-1CEa exposure resulted in profound morphological changes in Bcap-37 cells. The fluorescence imaging and flow cytometry analysis demonstrated that temporin-1CEa exhibited membrane-disrupting property characterized by induction of cell-surface phosphatidylserine exposure, elevation of plasma membrane permeability, and rapid transmembrane potential depolarization. Moreover, temporin-1CEa might also induce rapid cell death through mitochondria-involved mechanisms, including rapid intracellular Ca(2+) leakage, collapse of mitochondrial membrane potential (Δφm) and over-generation of reactive oxygen species (ROS). SIGNIFICANCE: In summary, the present study indicates that temporin-1CEa triggers a rapid cytotoxicity in Bcap-37 cells through membrane-destruction and intracellular mechanisms involving mitochondria. These intracellular mechanisms and direct membrane-destruction effect were evaluated helping to understand the detail action of antimicrobial peptides in mammalian cancer cells.