•  
  •  
 

Journal of Undergraduate Research

Keywords

anti-cancer, geldanamycin, Hsp-90, molecular structure

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

For my project I simulated the binding of geldanamycin in the ATP binding site of Heat shock protein-90 to assist Merritt Andrus’s research in designing a better anti-cancer drug. Hsp-90 is a protein found in the cells of many organisms including humans. It functions as a chaperone protein, helping other proteins assume their proper folded shape. When a ligand like geldanamycin binds to the active site on Hsp-90, the protein’s function is inhibited. In many cancer cells Hsp-90 is folded into a 3D shape that allows for easy binding with geldanamycin. A cancerous cell with inhibited Hsp-90 is far more likely to die because some other proteins in the cell are unable to fold without Hsp-90. As a result, injecting geldanamycin into an organism near a tumor has been found to be an effective targeted anti-cancer treatment.

Download

Included in

Chemistry Commons

Share

COinS