Unveiling the peptidome diversity of Lachesis muta snake venom: Discovery of novel fragments of metalloproteinase, l-amino acid oxidase, and bradykinin potentiating peptides
peer-reviewed · Biochemical and Biophysical Research Communications · 2023
| Date | 2023-11-01 |
| Type | peer-reviewed |
| Venue | Biochemical and Biophysical Research Communications |
| Publisher | Elsevier BV |
| Contribution | downstream-application |
| DOI | 10.1016/j.bbrc.2023.10.022 |
| Citations (OpenAlex) | 6 |
Abstract
Snake venoms are known to be major sources of peptides with different pharmacological properties. In this study, we comprehensively explored the venom peptidomes of three specimens of Lachesismuta, the largest venomous snake in South America, using mass spectrometry techniques. The analysis revealed 19 main chromatographic peaks common to all specimens. A total of 151 peptides were identified, including 69 from a metalloproteinase, 58 from the BPP-CNP precursor, and 24 from a l-amino acid oxidase. To our knowledge, 126 of these peptides were reported for the first time in this work, including a new SVMP-derived peptide fragment, Lm-10a. Our findings highlight the dynamic nature of toxin maturation in snake venoms, driven by proteolytic processing, post-translational modifications, and cryptide formation.
Methods and tools
- Lachesis muta venom peptidome: Peptidomic survey of bushmaster (Lachesis muta) venom using PEAKS de novo sequencing with database and homology searches, reporting 151 peptides, 126 of them new, including the metalloproteinase-derived fragment Lm-10a.
Methods it uses
Data deposited
- Lachesis muta snake venom peptidome — as deposited · PXD045732