Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis.
Chang ZhouZhengming WangXin PengYao LiuYangjun LinZhe ZhangYuling QiuMeihua JinRan WangDexin KongPublished in: Chemical biology & drug design (2017)
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.
Keyphrases
- amino acid
- mass spectrometry
- high throughput
- staphylococcus aureus
- soft tissue
- high resolution
- endothelial cells
- stem cells
- induced apoptosis
- wound healing
- emergency department
- oxidative stress
- risk assessment
- liquid chromatography
- multidrug resistant
- gram negative
- cell death
- electronic health record
- adverse drug
- genetic diversity