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Scripps scientists find structure of a protein that makes cancer cells resistant to chemotherapy
Date:3/26/2009

like the bacterial protein, the mammalian P-gp was designed to have a wide range of substrates," says Chang. "The presence of so many hydrophobic and aromatic residues explains how this happens."

A Path to Better Drugs

The new study also produced insights by showing structures of P-gp bound to some of its substrates. Chang and Aller collaborated with Qinghai Zhang, an assistant professor at Scripps Research, who had designed several compounds that can block the function of P-gp. These compounds bind inside the P-gp cavity, preventing other substances from entering. Chang and Aller were able to obtain the structures of two of Zhang's compounds inside P-gp.

"They both go in the same cavity and bind to different amino acids, but with some overlap," says Aller. "What this tells us is that there is an extremely important core set of amino acids in P-gp that bind all substances, and there are additional amino acids for fine-tuning the binding to specific drugs."

Knowing what the P-gp binding cavity looks like and precisely where substances bind may allow researchers design better drugs, for example by using chemistry to modify portions of that drug so that it can sneak past P-gp to get inside cells.

"[One advantage in this process is] we don't have to design brand new drugs, but rather re-design existing ones to make them work better," says Chang. "Scripps is a perfect place for these kinds of studies because there are great chemistry and biology labs here. We can easily find collaborators."


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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
Source:Eurekalert

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