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Suresh V. Ambudkar, Ph.D.

Portait Photo of Suresh Ambudkar
Laboratory of Cell Biology
Head, Transport Biochemistry Section
Deputy Laboratory Chief
Center for Cancer Research
National Cancer Institute
Building 37, Room 2120
Convent Drive
Bethesda, MD 20892-4256
Phone:  
301-402-4178
Fax:  
301-435-8188
E-Mail:  
ambudkar@mail.nih.gov

Biography

Dr. Ambudkar obtained his Ph.D. from Madurai Kamaraj University, Madurai, India, and received his postdoctoral training in membrane bioenergetics at the University of Maryland. He continued his postdoctoral work on biochemistry of membrane transport proteins at the Johns Hopkins University School of Medicine. In July 1995, after 5 years as an assistant professor in the departments of medicine and physiology at Johns Hopkins, he joined the Laboratory of Cell Biology at the CCR, NCI. He serves as Deputy Chief of the Laboratory of Cell Biology and Chief of the Transport Biochemistry Section.

Research

Project Title: Biochemistry of Multidrug Transporters

ATP-binding cassette (ABC) transporters such as P-glycoprotein (Pgp, ABCB1), the multidrug resistance-associated protein 1 (MRP1, ABCC1), and ABCG2 (MXR, BCRP), which function as ATP-dependent efflux pumps, play an important role in the development of multidrug resistance (MDR) in most cancers. Our current goals are to determine the mechanisms of action of multidrug resistance-linked ABC transporters including Pgp and ABCG2. We are addressing these questions: a) What is the molecular mechanism of the polyspecificity of Pgp? b) How do substrate binding and ATP sites interact? c) How is the energy from ATP hydrolysis used for drug transport? Our long-term goal is to elucidate the role of ABC drug transporters in the development of MDR in cancers and facilitate new therapeutic strategies.
Current work:
1. Elucidation of the catalytic cycle of ATP hydrolysis and transport pathway of Pgp and role of conserved motifs in the ATP-binding cassette.
2. Development of potent non-toxic small molecule modulators/inhibitors of ABC transporters.
3. Resolution of the three-dimensional structure of human Pgp.
4. Role of intracellular loops 1 and 3 in folding and stability of human Pgp:
These studies should provide insights into the mechanism of action and regulation of these transporters and aid in the development of strategies to increase the efficiency of chemotherapy to treat cancer.

This page was last updated on 4/18/2014.