Interference of Hsp90-p23 binding as a possible therapeutic treatment for cancer

CHED 866

Vi T. Tran, Vtran5@xula.edu1, Thao N. Tran, Ttran16@xula.edu2, Minh V. Tran2, Charles Miller III, rellim@tulane.edu3, and David E. Wolfgang, dwolfgan@xula.edu1. (1) Department of Chemistry, Xavier University of Louisiana, 1 Drexel Drive, New Orleans, LA 70125, (2) Department of Biology, Xavier University of Louisiana, New Orleans, LA 70125, (3) Department of Environmental and Health Sciences, Tulane University, 1430 Tulane Ave, New Orleans, LA 70112
Hsp90 is a heat shock protein that helps other proteins re-fold under stressful conditions, such as cancer. P23 is a co-chaperone of Hsp90, which binds to the protein and enhances its activity. In certain cancers, an elevated expression of Hsp90 and p23 helps mutated proteins retain their proper conformation, allowing for rapid cell growth. This complex is a potential target for the treatment of cancer. Preliminary results indicate that embryonic mice cells null for p23 are more susceptible to geldanamycin and herbimycin treatments. By interfering with the interaction of Hsp90 and p23, we hope to selectively increase the toxicity of the drugs towards cancer cells. The crystal structure of yeast p23 and Hsp90 complex is known. A rationally designed peptide will be produced to interfere with this interaction. The peptide will then be screened using a computer model. Peptides that show tight binding will be tested in-vitro.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008