Proteomics

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Lachesis muta snake venom peptidome


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 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.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Lachesis Muta

TISSUE(S): Venom

SUBMITTER: Alexandre Keiji Tashima  

LAB HEAD: Alexandre Keiji Tashima

PROVIDER: PXD045732 | Pride | 2023-10-23

REPOSITORIES: Pride

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Publications

Unveiling the peptidome diversity of Lachesismuta snake venom: Discovery of novel fragments of metalloproteinase, l-amino acid oxidase, and bradykinin potentiating peptides.

Ito Lucas T LT   Miyamoto Jackson G JG   Sant'Anna Sávio S SS   Grego Kathleen F KF   Tanaka-Azevedo Anita M AM   Tashima Alexandre K AK  

Biochemical and biophysical research communications 20231006


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 oxidas  ...[more]

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