Currently, there are two potential treatments for Parkinson’s disease: L-Dopa and a stimtrode inserted into the Globus Pallidus or subthalamic nuceli (Weaver FM, Follett K, Stern M, et al. JAMA. 2009;301(1):63–73.).  L-Dopa is by far the most common treatment for Parkinson’s as it is noninvasive and many Parkinson’s patients are older and unfit for invasive surgery, (Weaver FM, Follett K, Stern M, et al. JAMA. 2009;301(1):63–73.). In order to improve the effectiveness of L-Dopa as a treatment our current research is aimed at designing an inhibitor to both inhibit selectively the enzymes that may break down L-Dopa before it reaches the Blood Brain Barrier, while also safely bypassing the enzymes that are involved in the biosynthesis of dopamine. In order to determine the binding of this potential inhibitor to these enzymes, we must determine (among other things) the desolvation energy required to strip the waters from the active site and bind the inhibitor. To do this various enzymes related to the dopamine metabolism pathway such as ALDH and tyrosine hydroxylase were optimized in pm6 and m062x/3-21G with various numbers of water pairs in order to determine a trend in the desolvation energies. While large enzymes showed inconsistent results in pm6; m062x/3-21G showed more consistent results revealing a general ‘logarithmic’ trend in desolvation energy the more waters that were present in the active site.<br/>

Measuring the desolvation energy of the active-site of enzymes within the dopamingeric metabolic pathway

2019 Spring National Meeting

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