Peptide name : Hymenochirin-1B

Source/Organism : Zaire dwarf clawed frog

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: Not available

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : LDH release assay, MTT assay

Assay time : 24h

Activity : MIC : 0 - 50 μM

Cell line : H460

Cancer type : Lung cancer

Other activity : Anti-microbial activity

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Zhang Y, et al. Host defense peptide Hymenochirin-1B induces lung cancer cell apoptosis and cell cycle arrest through the mitochondrial pathway. Biochem Biophys Res Commun. 2019; 512:269-275. doi: 10.1016/j.bbrc.2019.03.029

Paper title : Host defense peptide Hymenochirin-1B induces lung cancer cell apoptosis and cell cycle arrest through the mitochondrial pathway.

Doi : https://doi.org/10.1016/j.bbrc.2019.03.029

Abstract : The antineoplastic activity of host defense peptide Hymenochirin-1B, has been extensively studied. However, the mechanism still remains unknown. In this study, linear peptide, Hymenochirin-1B, was synthesized via solid-phase peptide synthesis and evaluated for its anticancer efficacy. We found Hymenochirin-1B induced lung cancer cell apoptosis and cell cycle arrest at the G0/G1 phase. Moreover, Hymenochirin-1B could enter the cells and colocalized with mitochondria. Furthermore, decrease of mitochondrial membrane potential, increase of reactive oxygen species and the expression of apoptosis-associated protein (Bax/Bcl-2 ratio and activated Caspase-3) were observed in NCI-H1299 and A549 cells after Hymenochirin-1B treatment, suggesting that Hymenochirin-1B induced apoptosis via mitochondrial pathway. Our results provide new insights on the anticancer mechanism of Hymenochirin-1B, which may contribute to its further development into an antineoplastic drug in the future.