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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

An Evaluation of 3-Rhamnosylquercetin, a Glycosylated Form of Quercetin, against the Myotoxic and Edematogenic Effects of sPLA(2) from Crotalus durissus terrificus

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Toyama, Daniela de Oliveira [1] ; Gaeta, Henrique Hessel [2] ; Terashima de Pinho, Marcus Vinicius [2, 3] ; Pena Ferreira, Marcelo Jose [4] ; Romoff, Paulete [4] ; Matioli, Fabio Filippi [5] ; Magro, Angelo Jose [5] ; de Mattos Fontes, Marcos Roberto [5] ; Toyama, Marcos Hikari [2]
Total Authors: 9
[1] Univ Presbiteriana Mackenzie, CCBS, BR-01302907 Sao Paulo - Brazil
[2] UNESP, BIOMOLPEP, Lab Biol Mol & Peptideos, BR-11330900 Sao Vicente, SP - Brazil
[3] Univ Estadual Campinas, Fac Ciencias Med, Programa Posgrad Farmacol, BR-13083970 Campinas, SP - Brazil
[4] Univ Presbiteriana Mackenzie, Escola Engn, BR-01302907 Sao Paulo - Brazil
[5] UNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618970 Botucatu, SP - Brazil
Total Affiliations: 5
Document type: Journal article
Web of Science Citations: 3

This paper shows the results of quercitrin effects on the structure and biological activity of secretory phospholipase (sPLA(2)) from Crotalus durissus terrificus, which is the main toxin involved in the pharmacological effects of this snake venom. According to our mass spectrometry and circular dichroism results, quercetin was able to promote a chemical modification of some amino acid residues and modify the secondary structure of C. d. terrificus sPLA(2). Moreover, molecular docking studies showed that quercitrin can establish chemical interactions with some of the crucial amino acid residues involved in the enzymatic activity of the sPLA(2), indicating that this flavonoid could also physically impair substrate molecule access to the catalytic site of the toxin. Additionally, in vitro and in vivo assays showed that the quercitrin strongly diminished the catalytic activity of the protein, altered its Vmax and Km values, and presented a more potent inhibition of essential pharmacological activities in the C. d. terrificus sPLA(2), such as its myotoxicity and edematogenic effect, in comparison to quercetin. Thus, we concluded that the rhamnose group found in quercitrin is most likely essential to the antivenom activities of this flavonoid against C. d. terrificus sPLA(2). (AU)

FAPESP's process: 12/06502-5 - Structural and functional studies of native, recombinant and complexed proteins, from snake venom, with vegetable inhibitors
Grantee:Marcos Roberto de Mattos Fontes
Support Opportunities: Regular Research Grants
FAPESP's process: 13/12077-8 - Evaluation of leaf extracts of Laguncularia racemosa on enzymatic and pharmacological activities of Phospholipases A2 from snake venom
Grantee:Daniela de Oliveira Toyama
Support Opportunities: Regular Research Grants
FAPESP's process: 11/06704-4 - Characterization of anti-phospholipase A2 activity and evaluation of potential anti-inflammatory of natural and modified special metabolites from plants
Grantee:Marcos Hikari Toyama
Support Opportunities: Regular Research Grants