Group IV cytosolic phospholipase A2¦Á (cPLA2¦Á) hydrolyzes membrane phospholipids to produce arachidonic acid and lysolipid. The C2 domain of the enzyme is involved in the Ca2+ dependent translocation of the enzyme to the membrane and has a structure of 8 anti-parallel ¦Â sheets composed of 132 amino acids. Ceramide-1-phosphate (C1P) enhances the association of the C2 domain with membranes. This research project aims to understand the binding properties and secondary structural changes of the cPLA2¦Á C2 domain in the presence of phosphatidylcholine (PC). We optimized the protein expression conditions to obtain the cPLA2¦Á C2 domain un-aggregated and in sufficient quantity. Initial FTIR-ATR experiments confirmed the ¦Â-sheet structure of the protein alone and in the presence of PC.
Worcester Polytechnic Institute
Major Qualifying Project
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Chemistry and Biochemistry