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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<jats:italic>C. d. terrificus<\/jats:italic>sPLA<jats:sub>2<\/jats:sub>. 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<jats:sub>2<\/jats:sub>, indicating that this flavonoid could also physically impair substrate molecule access to the catalytic site of the toxin. Additionally,<jats:italic>in vitro<\/jats:italic>and<jats:italic>in vivo<\/jats:italic>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<jats:italic>C. d. terrificus<\/jats:italic>sPLA<jats:sub>2<\/jats:sub>, 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<jats:italic>C. d. terrificus<\/jats:italic>sPLA<jats:sub>2<\/jats:sub>.<\/jats:p>","DOI":"10.1155\/2014\/341270","type":"journal-article","created":{"date-parts":[[2014,2,18]],"date-time":"2014-02-18T21:01:57Z","timestamp":1392757317000},"page":"1-11","source":"Crossref","is-referenced-by-count":14,"title":["An Evaluation of 3-Rhamnosylquercetin, a Glycosylated Form of Quercetin, against the Myotoxic and Edematogenic Effects of sPLA<sub>2<\/sub>from<i>Crotalus durissus terrificus<\/i>"],"prefix":"10.1155","volume":"2014","author":[{"given":"Daniela de Oliveira","family":"Toyama","sequence":"first","affiliation":[{"name":"Centro de Ci\u00eancias Biol\u00f3gicas e da Sa\u00fade (CCBS), Universidade Presbiteriana Mackenzie, 01302-907 S\u00e3o Paulo, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Henrique 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