Peptide name : Bombinin H-BO

Source/Organism : Oriental Fire-bellied Toad

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 17

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 48h

Activity : IC50 : 3.87μM

Cell line : Hep G2

Cancer type : Human hepatoma

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1604.029 Dalton

Aliphatic index : 2.064

Instability index : 23.0059

Hydrophobicity (GRAVY) : 1.8235

Isoelectric point : 8.7501

Charge (pH 7) : 0.7591

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 16

hydrophobic moment : 0.3527

Missing amino acid : C,R,W,H,Q,T,M,E,F,S,D,Y,N

Most occurring amino acid : G

Most occurring amino acid frequency : 5

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.5)

SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)CC)C(C)C)[C@@H](C)CC

1 : Zhou C, et al. Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. Chem Biol Drug Des. 2018; 91:50-61. doi: 10.1111/cbdd.13055

Paper title : Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis.

Doi : https://doi.org/10.1111/cbdd.13055

Abstract : Amphibian skin secretions are known to contain numerous peptides with a large array of biological activities. Bombinins are a group of amphibian-derived peptides with broad spectrum antimicrobial activities that have been only identified from the ancient toad species, Bombina. In this study, we described the identification and characterization of a novel bombinin precursor which encoded a bombinin-like peptide (BLP-7) and a novel bombinin H-type peptide (named as Bombinin H-BO) from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. The primary structures of both mature peptides were determined by combinations of molecular cloning of peptide precursor-encoding cDNAs and mass spectrometry techniques. Secondary structure prediction revealed that both peptides had cationic amphipathic α-helical structural features. The synthetic replicate of BLP-7 displayed more potent antimicrobial activity than Bombinin H-BO against Gram-positive and Gram-negative bacteria and yeast. Also, in vitro antitumour assay showed that both peptides possessed obvious antiproliferative activity on three human hepatoma cells (Hep G2/SK-HEP-1/Huh7) at the non-toxic doses. These results indicate the peptide family of bombinins could be a potential source of drug candidates for anti-infection and anticancer therapy.