Peptide name : Caspase 3 inhibitor

Source/Organism : Caspase 3 inhibitor

Linear/Cyclic : Linear

Chirality : L

Peptide length: 4

C-terminal modification: Linear

N-terminal modification : Fluoromethyl ketone(fmk)

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 1h

Activity : 65% cytotoxicity at 30 µM

Cell line : Bcap-37

Cancer type : Breast cancer

Other activity : Anti-microbial

Amino acid composition bar chart :

Molecular mass : 476.4351 Dalton

Aliphatic index : 0.725

Instability index : -30.075

Hydrophobicity (GRAVY) : -1.575

Isoelectric point : 4.05

Charge (pH 7) : -3.2317

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 0.33333333

hydrophobic moment : -2.147

Missing amino acid : W,T,P,I,M,K,F,N,G,C,R,H,Q,S,Y,L,A

Most occurring amino acid : D

Most occurring amino acid frequency : 2

Least occurring amino acid : E

Least occurring amino acid frequency : 1

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

SMILES Notation: CC(C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](N)CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O

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.