Research


Current research with Prof. Jorgensen involves the study of selective factor Xa inhibitors, and their relative binding affinities to factor Xa.
Ribbon diagram of factor Xa with active site residues shown in green.

Factor Xa is a serine protease in the blood coagulation cascade whose main function is to convert prothrombin into thrombin. Thrombin then goes on to catalyze reactions that result in the formation of fibrin, the main constituent of all blood clots in the body. Since factor Xa links the intrinsic and extrinsic pathways of blood coagulation, its inhibition can prevent thrombin formation via either route.


Solvent accessible surface of the active site in Factor Xa.
The S4 (aryl) binding pocket is in purple, the S1 (amidine) binding pocket is in red, the catalytic triad is in yellow.

We use the Monte Carlo/Extented Linear Response (MC/ELR) methodolgy to elucidate factors important in conferring high-affinity binding to factor Xa. These studies can provide insight into the design of more potent inhibitors.