Abstract
Understanding snake venom kinetics is crucial for developing risk evaluation strategies and determining the best dose and timing of antivenom required to bind all venom in snakebite patients. Polyphenolic compounds have shown to inhibit toxic effects induced by snake venom proteins. The interaction of polyphenols with Phospholipase A2 of Cerastes cerastes snake venom was investigated by fluorescence spectroscopy. The decrease in the fluorescence versus time was conducted at room temperature in 0.01 M Tris, 0.1 M NaCl at pH 7.4. The decrease in fluorescence was following a pattern of zero-order kinetics rate in which the fluorescence is decreasing linearly with time. This study is expected to offer additional information about the interactions of PLA2 with natural product that might lead to therapeutic drug
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