Unveiling the Diversity and Modifications of Short Peptides in IButhus martensii/I Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry

• Published in: Toxins 2024-03, Vol.16 (3)
• Main Authors: Zeng, Ling, Zhang, Cangman, Yang, Mingrong, Sun, Jianfeng, Lu, Jingguang, Zhang, Huixia, Qin, Jianfeng, Zhang, Wei, Jiang, Zhihong
• Format: Article
• Language: English
• Subjects: Chemical properties; Chemical research; High performance liquid chromatography; Mass spectrometry; Peptides; Post-translational modification; Scorpions; Structure; Venom
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins16030155

More recently, short peptides in scorpion venom have received much attention because of their potential for drug discovery. Although various biological effects of these short peptides have been found, their studies have been hindered by the lack of structural information especially in modifications. In this study, small peptides from scorpion venom were investigated using high-performance liquid chromatography high-resolution mass spectrometry followed by de novo sequencing. A total of 156 sequences consisting of 2~12 amino acids were temporarily identified from Buthus martensii scorpion venom. The identified peptides exhibited various post-translational modifications including N-terminal and C-terminal modifications, in which the N-benzoyl modification was first found in scorpion venom. Moreover, a short peptide Bz-ARF-NH[sub.2] demonstrated both N-terminal and C-terminal modifications simultaneously, which is extremely rare in natural peptides. In conclusion, this study provides a comprehensive insight into the diversity, modifications, and potential bioactivities of short peptides in scorpion venom.