Research Final Summary

Final Summary

In the end, we investigated five molecules for inhibition of Pyruvate Kinase. Of the five, two definitively inhibit PK. One definitively does not inhibit PK. Finally, two of them might inhibit PK and need to be tested further.

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June 18-26 Pyruvate Kinase Inhibition

Pyruvate Kinase Inhibition Continued

With the chosen method to determine the activity of pyruvate kinase, there are two stages where time can be varied. Initially, I tested the inhibition of pyruvate kinase after varying the time at both stages. Each molecule must also be tested at multiple concentrations. There were just too many variables of interest.

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June 7-14 Pyruvate Kinase Inhibition

Use of Molecules to Inhibit Pyruvate Kinase

With a method to measure the activity of pyruvate kinase, the research could begin. Next, the goal was to investigate the effects of various molecules on the activity of pyruvate kinase. This had to be done in three stages. In the first stage, the molecule modifies pyruvate kinase. In the second stage pyruvate kinase is allowed to react. Finally, in the third stage, a simple reaction occurs to make the product from stage 2 measurable.

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May 30- June 6 Establishing Controls

Stability of Relevant Molecules

For the first 2 weeks of summer research, the goal has been to lay the groundwork for the rest of the summer. The amount of time certain molecules can sit out on the lab top at room temperature before they degrade and become unusable had to be established. Then the effect of freezing and thawing an enzyme multiple times on its activity level was investigated. These things had to happen before the real research could begin. This took several days of control experiments.

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The goal of this research is to study the reaction rates of tyrosinase and pyruvate kinase under various reaction conditions. Pyruvate kinase is an enzymes found in humans and is an important energy producing enzyme involved in the metabolism of glucose. Currently, research is focused on preliminary studies of an enzyme called tyrosinase that catalyzes the formation of melanin which is a molecule that acts as protection against UV light. First the uninhibited reaction rate of tyrosinase with dopamine, L-DOPA, and caffeic acid will be studied. Then the reaction rates of the pyruvate kinase will also be investigated. Both enzymes will be studied in the presence of oxidative molecules. The interest in pyruvate kinase comes from its potential to act as a protector for other proteins necessary for cellular function against oxidative damage. When accumulated in many types of critical proteins, oxidative damage can lead to neurodegenerative diseases, such as Alzheimer’s disease.