Group IV cytosolic phospholipase A2Á (cPLAZÁ) 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  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 cPLA2Á C2 domain in the presence of phosphatidylcholine (PC). We optimized the protein expression conditions to obtain the cPLA2Á 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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Sun, Yunqiu

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-050114-130049

Advisor

• Gericke, Arne

Year

• 2014

Date created

• 2014-05-01

Resource type

• Major Qualifying Project

Major

• Chemistry

Rights statement

• In Copyright