Enzyme inhibition, drug design

Inhibition of enzymatic reactions by transition state analogs has been an extremely important approach for drug design [20], the principle underlying this is that "nature has developed enzymes for binding efficiently to the transition states of the reactions they catalyse". 

Ghanbari, F., Rowland-Yeo, K.. Bloomer. J.C., Clarke, S.E., Lennard, M.S., Tucker, G.T. and Rostami-Hodjegan, A. (2006) A critical evaluation of the experimental design of studies of mechanism based enzyme inhibition, with implications for in vitrO in vivo extrapolation. Current Drug Metabolism, 1, 315-334. 

Class of drugs designed to inhibit the enzyme protease. 

Most reversible inhibitors may be further classified as being either competitive, non-competitive or uncompetitive. In competitive inhibition the inhibitor usually binds by a reversible process to the same active site of the enzyme as the substrate. Since the substrate and inhibitor compete for the same active site it follows that they will probably be structurally similar (Figure 7.3). This offers a rational approach to drug design in this area. 

---