Project description: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 Lachesis muta, 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.

2023-10-23 | PXD045732 | Pride

Mus musculus strain:Muta(tm)Mouse

Project description:BaP mutations induced in the Muta(tm)mouse lacZ transgene

| PRJNA284951 | ENA

Project description:Prokaryotic community analysis of the marine sponges Xestospongia muta and Agelas sventres along a depth gradient

| PRJNA453745 | ENA