In addition to peptides with disulfide bonds, scorpion venom contains linear peptides without disulfide bonds. Many of these linear peptides have amphipathic α-helical structures, often have antimicrobial activity, and can be classified into three groups based on molecular size. In particular, long-chain antimicrobial peptides with more than 40 residues are difficult to synthesize, and therefore have not been sufficiently studied. We previously reported transcriptome analysis of the venom gland. Riojeres australasiae This revealed the precursor sequence of a long-chain antimicrobial peptide. In the study reported here, we identified the mature structure of one such long-chain antimicrobial peptide, LaCT1, and synthesized it using chemical ligation to confirm its structure and assess its biological activity. did. The results showed that LaCT1 exhibited significant antibacterial activity. Furthermore, we identified partial peptides consisting of N-terminal or C-terminal regions that could be generated by enzymatic cleavage in the venom. Among these, only the peptide containing the N-terminal half region showed activity. LaCT1 not only exhibited insecticidal activity but also synergistically enhanced the effects of other insecticidal peptides identified in LaCT1. L. Australasie Poison too. These results provide insight into the role of antimicrobial peptides in scorpion venom.
Masaki Miyashita, Shinji Sakai, Tatsuya Okabe, Susumu Kawai, Tetsuya Kishimoto, Akira Kitanaka, Naoki Mitani, Yuya Nakagawa, Identification and synthesis of long-chain antimicrobial peptides from the venom of Liocheles australasiae scorpion. Peptide Science Journale3661. https://doi.org/10.1002/psc.3661
