Unveiling the Diversity and Modifications of Short Peptides in Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry
peer-reviewed · Toxins · 2024
| Date | 2024-03-16 |
| Type | peer-reviewed |
| Venue | Toxins |
| Publisher | MDPI |
| Contribution | downstream-application |
| DOI | 10.3390/toxins16030155 |
| Citations (OpenAlex) | 6 |
| Venue 2-year citedness | 3.89 |
Abstract
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-NH2 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.
Methods and tools
- Scorpion venom short peptides: LC-HRMS with de novo sequencing of short (2-12 aa) scorpion venom peptides: 156 sequences identified, revealing N- and C-terminal modifications including the previously unreported N-benzoyl modification.
Cites (2)
- De novo sequencing of proteins by mass spectrometry (2020) both
- De novo sequencing of peptides by MS/MS (2010) both