Research

Funded Projects:

Ongoing: "Characterization of Novel Mutants of Human Protein Z-dependent Protease Inhibitor (ZPI): Potential Therapeutics for Hemophilia" funded by SERB (CRG/2021/002239). Sanctioned amount: 60,46,392/-

Completed: "Understanding the Structure Function Relationship of the Natural Anticoagulant ZPI, a Member of Serpin Superfamily" funded by SERB (ECR/2017/000447). Sanctioned amount : 34,62,800/-

We are working on human PZ (Protein Z) - ZPI (Protein Z dependent Serine Protease Inhibitor), an important natural anticoagulant system of our body.

ZPI, a member of serpin (serine protease inhibitor) superfamily, inhibits the clotting factor fXa in presence of its cofactor PZ, and, pro-coagulant Ca²+ and anionic phospholipids. Unlike the other relatively well studied serpins, little is known about the stability, folding-misfolding, polymerization and inhibitory mechanism of ZPI.

Therefore we are interested to

1. probe the nature of folding energy landscape of ZPI and how it is altered by structurally important and clinically relevant ZPI mutants;

2. understand the exact physiological role of PZ/ZPI system in various pathophysiological conditions specially in cancer;

3. study the formation of ternary complex (fXa-PZ-ZPI) on lipid membrane.

Other research interest include the study of the interaction of various signal peptides with lipid membranes.