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Updated: Aug 15, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
Direct antimicrobial activities of PR-bombesin
Jianxu Li1, Xueqing Xu, Haining Yu
1Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
Abstract:
PR-bombesin is a bombesin-like peptide derived from the skin of the Chinese red belly toad, Bombina maxima. The 8-residue segment of N-terminal of RP-bombesin, comprising four prolines and three basic residues, is extensively different from other bombesin-like peptides. Since sequence of Pro-Arg-Pro generally plays an important role in the antimicrobial activity of proline-rich antimicrobial peptides, the componential feature of PR-bombesin indicates that it may have antimicrobial activity. In this paper, we presented the first evidence that bombesin-like peptides possess direct antimicrobial activities as some neuropeptides. It was determined by CD spectroscopy that PR-bombesin adopted a combination of random coil and beta-sheet structure, suggesting RP-bombesin is a new member of antimicrobial peptides having beta structure but without disulfide bonds. Current results also supported that PR-bombesin plays a direct defensive role besides its neuro-endocrological functions.
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