Proteomics

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A novel peptide from Bothrops cotiara peptidome

ABSTRACT: The knowledge regarding toxins diversity, composition, structure, molecular and pharmacological interactions involved in the process of envenomation provide lessons for drug design based on these natural molecular scaffolds and pharmacophores of toxins. This study unravels new toxins sequenced by mass spectrometry analysis of Bothrops cotiara peptidome, and the potential biological activities of these toxins were explored.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Bothrops Cotiara

TISSUE(S): Venom

SUBMITTER: Alexandre Keiji Tashima  

LAB HEAD: Alexandre Keiji Tashima

PROVIDER: PXD041473 | Pride | 2023-10-20

REPOSITORIES: Pride

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Publications

Snake venoms are primarily composed of proteins and peptides, which selectively interact with specific molecular targets, disrupting prey homeostasis. Identifying toxins and the mechanisms involved in envenoming can lead to the discovery of new drugs based on natural peptide scaffolds. In this study, we used mass spectrometry-based peptidomics to sequence 197 peptides in the venom of Bothrops cotiara, including a novel 7-residue peptide derived from a snake venom metalloproteinase. This peptide,  ...[more]

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