Abstract
Phospholipase A2 (PLA2) represents a major venom component of snakes and bees and exhibits a broad range of biological effects including myotoxicity, neurotoxicity, hemolysis, cardiotoxicity, anticoagulant and antiplatelet activities. Melittin, is the main component and the major pain producing substance of honeybee venom. The aim of the present study was to differentiate between snake and bee venoms using Aqueous Olive Leaf Extract (AOLE) employing fluorescence techniques. Tryptophan, which is contained in both snake and bee venoms is fluorescent at UV wavelength and hence widely used as a tool to monitor conformational changes in proteins and to draw inferences regarding local structure and dynamics. Fluorescence spectroscopy and molecular modeling have been used to analyze enzyme activity in the absence and presence of AOLE and to verify potential binding of AOLE components to the enzyme. Changes in the fluorescence intensities with blue and red shifts were obtained with bee and snake venoms, respectively. Binding of AOLE constituents near the active site of the enzyme could be evidenced and possible modes of interaction are discussed. The fluorescence method used was rapid and sensitive and was able to differentiate between snake and bee venoms utilizing AOLE.
Highlights
Libya and surrounding countries are inhabited by numerous venomous snakes of medical importance
The fluorescence spectrum shows a decrease of fluorescence intensity (Figure 1) of the snake venom due to addition of 100μl of Aqueous Olive Leaf Extract (AOLE) which could be related to various processes
The decrease in fluorescence emission intensity (Figure 2) was accompanied by a blue shift of 24 nm of the maximum emission (352 to 328nm) and this may indicate that binding of AOLE components may have accomplished a conformational change that moves Trp into a relatively more hydrophobic region
Summary
Libya and surrounding countries are inhabited by numerous venomous snakes of medical importance. Venoms from snakes within the family Viperidae are complex biochemical mixtures that function to immobilize the prey and initiate digestion. Cerastes cerastes venom contains many enzymes showing proteolytic activity and causes multiple kinds of intoxications [2]. Phospholipases A2 (PLA2) from Cerastes cerastes for example, has been associated with numerous toxicities including neurotoxicity, nephrotoxicity, lung toxicity, hepatotoxicity, and cardiotoxicity [3-5]. The lethal effect of snake venom mainly results from its active ingredients such as phospholipase A2 (PLA2). Phospholipid hydrolysis by PLA2 releases arachidonic acid whose metabolism results in the formation of potentially toxic Reactive Oxygen Species (ROS) and lipid peroxides [5,6]. The increase in the activity of liver enzymes indicating the damage of heart, liver and other organs could be attributed to the synergistic action of the venom components [2,5]
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