Inhibitors of biological enzymes are frequently produced by mimicking the molecular structure of the enzyme's natural substrate. Because of the extensive studies that have already been performed on the trypsin enzyme, its natural substrates and its mode of interaction with them are well understood. By finding an easily synthesized molecule to inhibit the trypsin enzyme, college level laboratory experiments could be designed and integrated into organic chemistry and biochemistry courses. In this project, a possible trypsin inhibitor molecule, 4-fluorobenzylaimine, was chosen based on its similarity to the natural trypsin substrates and because it has been predicted through computational studies to be a potential trypsin inhibiotr. 4-fluorobenzylaimine was synthesized and tested for inhibition using Michaelis-Menten kinetics. The inhibition constant, Ki, determined experimentally for a standard 4-fluorobenzylaimine was found to be 0.65 mM, which compared closely to the Ki calculated by Kurinov and Harrison. However, the Ki determined experimentally for the synthesized 4-fluorobenzylaimine was found to be 3.2 mM.
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Schneider, Eric L., "Synthesis and Characterization of a Trypsin Inhibitor" (1998). Honors Theses. 650.