In:
Chemical Biology & Drug Design, Wiley, Vol. 91, No. 1 ( 2018-01), p. 50-61
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 cDNA s 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.
Type of Medium:
Online Resource
ISSN:
1747-0277
,
1747-0285
DOI:
10.1111/cbdd.2018.91.issue-1
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
2216600-2
SSG:
12
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