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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):

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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	20191220_LM1_Lucas_DDA_001.mzML	Mzml
	20191220_LM1_Lucas_DDA_001.raw.zip	Raw
	20191220_LM1_Lucas_DDA_002.mzML	Mzml
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	20191220_LM1_Lucas_MSE_001.mzML	Mzml

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Publications

Effect of immobilization stress on histological, histochemical and electron-microscopic changes in porcine myocardium.

Wutzen J J Lewicki Z Z Rózycka Z Z Ceremuzyński L L Barcikowski R R

Materia medica Polona. Polish journal of medicine and pharmacy 19870401 2

PMID: 3448422

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