Snake venoms are complex mixtures of pharmacologically active proteins and polypeptides interfering in various physiological systems. They have been studied in search of the molecular basis of toxicity, have provided important biological tools to investigate vital physiological processes, and even have been used as therapeutic agents.
The neurotoxin Vipoxin is isolated from the venom of the Bulgarian viper Vipera ammodytes meridionalis. Structurally Vipoxin represents a heterodimeric postsynaptic ionic complex composed of two protein subunits— a basic and strongly toxic secretory phospholipase A2 (sPLA2) enzyme and an acidic, enzymatically inactive and nontoxic component, originally named Inhibitor.
My talk will be divided into two parts:
In the first one I will present my research concerning the action of the Vipoxin or its components on model membrane systems- phospholipid monolayers and bilayers. I will demonstrate how as a model system the classical Langmuir monolayer could be used for studying the enzyme hydrolysis and how the Michaelis-Menten kinetic model is modified in order to be obtained important kinetic constants of the enzyme reaction. In this part of my talk I will also show how AFM can be used as an analytical tool to visualize the degradation of a phospholipid bilayer by the vipoxin.
In the second part of my talk I will present our recent results obtained at WPI during my four months stay here as a Fulbright scholar which are part of my project, “Atomic Force Microscopy for studying the mechanical response of living cells exposed to the action of viper toxin (Vipoxin)”.
Refreshments will be served in Olin Hall 118 at 3:30 P.M.