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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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A novel metalloproteinase-derived cryptide from Bothrops cotiara venom inhibits angiotensin-converting enzyme activity.

Miyamoto Jackson Gabriel JG Kitano Eduardo Shigueo ES Zelanis André A Nachtigall Pedro Gabriel PG Junqueira-de-Azevedo Inácio I Sant'Anna Sávio Stefanini SS Lauria da Silva Rogério R Bersanetti Patrícia Alessandra PA Carmona Adriana Karaoglanovic AK Barbosa Pereira Pedro José PJ Serrano Solange M T SMT Vilela Oliva Maria Luiza ML Tashima Alexandre Keiji AK

Biochimie 20231014

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]

PMID: 37839625

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