Publication Date
12-2011
Advisor(s) - Committee Chair
Dr. Kevin Williams (Director), Dr. Bangbo Yan,Dr. Eric Conte
Degree Program
Department of Chemistry
Degree Type
Master of Science
Abstract
The anticancer activity of several platinum compounds is due to the formation of complexes with DNA. We hypothesize that the size and shape of the platinum compounds would impact interaction with proteins, and these interactions may be partly responsible for the anticancer activity. Chymotrypsin and subtilisin are serine proteases that have a histidine residue in the active site. We are investigating the inhibition of the digestive enzymes chymotrypsin and subtilisin by analogs of the anticancer drug cisplatin and trying to discern trends in the inhibition as the active site residues vary. In our research, we found that the enzyme subtilisin did not show any significant inhibition with different platinum compounds we used, while chymotrypsin showed inhibition only with the potassium tetrachloroplatinate and this inhibition is concentration dependent
Disciplines
Genetic Processes | Medicinal-Pharmaceutical Chemistry
Recommended Citation
Ravipati, Dhatri, "Activity of Analogs of Anticancer Drugs on the Serine Protease Enzymes Subtilisin and Chymotrypsin" (2011). Masters Theses & Specialist Projects. Paper 1134.
https://digitalcommons.wku.edu/theses/1134