Hartings AU Phosphorylation Lab: Difference between revisions

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{{Template:Hartings AU Phosphorylation Lab}}
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The American University Biomaterials Design Lab is a student run and operated laboratory course in the department of chemistry. Our goal is to develop methodology for the chemical modification of biocompatible materials and to tailor these new materials for medical and biotechnological applications. Our first semester of research will be the Fall of 2011. The efforts of this first semester will expand off of the work done developing protein films by Bakshi, ''et al'' ([[doi:10.1021/jp110296y]]). In this work, the authors synthesize a gold nanoparticle that is templated and solubilized by the protein bovine serum albumin (BSA). They then create a biocompatible film that encapsulates these gold nanoparticles. We will be developing techniques for chemically modifying the protein that encapsulates the gold nanoparticle and will test these methodologies on the nanoparticles while in solution and while in a film.<br>
We are synthesizing novel ruthenium-modified adenosine triphosphate (ATP) analogues. These molecules are being designed so that they can be used by kinases to phosphorylate protein-substrates with a ruthenium-modified phosphate group. Additionally, the ruthenated-phosphate group must be inaccessible to phosphatases such that once the protein-substrate is irreversibly phosphorylated. We plan to use these molecules to study and disrupt intracellular communication with a specific focus on cancerous cells. (The image above shows that one of the ruthenium-modified ATP molecules will look like (left) as well as a rendering of a protein structure with a tyrosine that has been phosphorylated with our modified ATP (right)). You can find more information on this lab at our group [http://hartingslab.com/research/phosphorylation website].<br>
<div style="text-align: center;">[[Image:AU BDLabs 1.png|450px]]</div><br>
<div style="text-align: center;">[[Image:Hartings_Kinase_phosphatase_s.png|450px]]</div><br>
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Latest revision as of 10:35, 27 January 2012



We are synthesizing novel ruthenium-modified adenosine triphosphate (ATP) analogues. These molecules are being designed so that they can be used by kinases to phosphorylate protein-substrates with a ruthenium-modified phosphate group. Additionally, the ruthenated-phosphate group must be inaccessible to phosphatases such that once the protein-substrate is irreversibly phosphorylated. We plan to use these molecules to study and disrupt intracellular communication with a specific focus on cancerous cells. (The image above shows that one of the ruthenium-modified ATP molecules will look like (left) as well as a rendering of a protein structure with a tyrosine that has been phosphorylated with our modified ATP (right)). You can find more information on this lab at our group website.


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