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

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, named Bc-7a, features a pyroglutamic acid at the N-terminal and a PFR motif at the C-terminal, homologous to bradykinin. Using FRET (fluorescence resonance energy transfer) substrate assays, we demonstrated that Bc-7a strongly inhibits the two domains of angiotensin converting enzyme (Ki < 1 μM). Our findings contribute to the repertoire of biologically active peptides from snake venoms capable of inhibiting angiotensin-converting enzyme (ACE), beyond current known structural motifs and precursors. In summary, we report a novel snake venom peptide with ACE inhibitory activity, suggesting its potential contribution to the hypotensive effect observed in envenomation.PMID:37839625 | DOI:10.1016/j.biochi.2023.10.010

Source: Biochimie - October 15, 2023 Category: Biochemistry Authors: Jackson Gabriel Miyamoto Eduardo Shigueo Kitano Andr é Zelanis Pedro Gabriel Nachtigall In ácio Junqueira-de-Azevedo S ávio Stefanini Sant'Anna Rog ério Lauria da Silva Patr ícia Alessandra Bersanetti Adriana Karaoglanovic Carmona Pedro Jos é Barbos Source Type: research