Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents.
Journal
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas
ISSN: 1414-431X
Titre abrégé: Braz J Med Biol Res
Pays: Brazil
ID NLM: 8112917
Informations de publication
Date de publication:
2020
2020
Historique:
received:
27
06
2019
accepted:
31
10
2019
entrez:
16
1
2020
pubmed:
16
1
2020
medline:
23
2
2020
Statut:
epublish
Résumé
Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms.
Identifiants
pubmed: 31939598
pii: S0100-879X2020000100610
doi: 10.1590/1414-431X20199001
pmc: PMC6967130
pii:
doi:
Substances chimiques
Proteins
0
Proteome
0
Viper Venoms
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
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