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Huihui Xu Yang Zhang Xin Feng Kunyuan Tie Yuan Cao Wenyu Han 《Biotechnology letters》2017,39(6):897-903
Objectives
To identify and characterize a novel antimicrobial peptide, catesbeianin-1.Results
Catesbeianin-1 is 25 amino acids long and is α-helical, cationic and amphipathic. It had antimicrobial activity against Gram-positive and Gram-negative bacteria. It was resistant against trypsin and pepsin. Catesbeianin-1 exhibited moderate hemolytic activity (approx 8%) at 100 μg/ml, and its HC50 (50% hemolytic concentration) was 300 μg/ml. Its cytotoxicity was approx 10–20% at 100 μg/ml, and its CC50 (50% cytotoxic concentration) was >100 μg/ml. The LD50 of catesbeianin-1 in mice was 80 mg/kg. At 3.1 µg/ml, catesbeianin-1 significantly inhibited the growth of methicillin-resistant Staphylococcus aureus.Conclusions
A new antimicrobial peptide from the skin of Lithobates catesbeianus (American bullfrog) may represent a template for the development of novel antimicrobial agents.16.
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