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Analysis of the mechanism of novel cancer drug, KU177, on Aha1

Analysis of the mechanism of novel cancer drug, KU177, on Aha1

Garret Boren

Biochemistry & Molecular Biology

Cancer continues to cause problems throughout the world today. Despite the constant influx of new treatments and medications, cancer continues to be a leading cause of death. Cancer cells need specific proteins to function and replicate. One such protein is 90kDa heat shock protein (Hsp90), which is necessary for each of the original 6 hallmarks of cancer. Another protein, activator of Hsp90 ATPase 1 (Aha1), is necessary for Hsp90 function in cancer cells and thus has become a popular target in cancer drug development. This study looks at the effects of a novel Aha1 inhibitor, KU177, on the structure of Aha1 and in particular its C-terminal domain. Previous experiments have shown that KU177 interacts with the C-terminal domain of Aha1 (Aha1C), but these experiments had undefined issues likely due to the structure of the purified Aha1C clone. This presentation shows these previous experiments and purification methods of a newer Aha1C clone. The results indicate that KU177 interacts specifically at Aha1C and that a new clone of Aha1C was completely purified. These results provide a necessary starting step for more specific structural studies of the mechanism of KU177 using X-ray crystallography. This study also provides useful information on the mechanism of KU177, which can be useful in its later use as an anti-cancer medication. Results from these experiments will be useful as tools for researchers and medical doctors in future drug development and prescription.