Difference between revisions of "Team:TU Dresden/Project/"

 
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<h1>Project</h1>
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<p style="line-height:1.8"> We have subdivided the <i>Project</i> section in seven different parts:</p>
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<p style="line-height:1.8"> Protein-protein interactions play a key role in biology. Designing and coordinating interactions in order to discover new drugs comes with a host of challenges. Our goal is to modify phage-assisted continuous evolution (PACE), specifically for protein interactions. PACE combines the bacteriophage M13 and <i>Escherichia coli</i> in a dynamic scheme whereby M13 only survives if it infects <i>E. coli</i>. This is achieved when the viral protein P3 is expressed. <b>SPACE-P</b> aims to incorporate a key-lock mechanism that regulates the expression of P3. In our model, the interaction between the protein HER2 and an affibody will be the key to open the lock. Over several phage life cycles, evolutionary pressure will favour the interactions with the greatest yield of P3, thereby increasing that phages virulence and the continued evolution of that particular affibody. Our method will reduce the time and cost of drug discovery and enable the interaction between many choose-able proteins. </p>
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<h2>Do you want to know more about our project?</h2>
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<p style="line-height:1.8"> We have subdivided the <i>Project</i> section in six different parts:</p>
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<li style="margin-bottom: 10px;line-height:1.8;"><a style="text-decoration:none;" href="https://2015.igem.org/Team:TU_Dresden/Project/Overview"><font color="#045FB4">Overview</font></a></li>
 
<li style="margin-bottom: 10px;line-height:1.8;"><a style="text-decoration:none;" href="https://2015.igem.org/Team:TU_Dresden/Project/Description"><font color="#045FB4">Description</font></a></li>
 
<li style="margin-bottom: 10px;line-height:1.8;"><a style="text-decoration:none;" href="https://2015.igem.org/Team:TU_Dresden/Project/Description"><font color="#045FB4">Description</font></a></li>
 
<li style="margin-bottom: 10px;line-height:1.8;"><a style="text-decoration:none;" href="https://2015.igem.org/Team:TU_Dresden/Project/Background"><font color="#045FB4">Background</font></a></li>
 
<li style="margin-bottom: 10px;line-height:1.8;"><a style="text-decoration:none;" href="https://2015.igem.org/Team:TU_Dresden/Project/Background"><font color="#045FB4">Background</font></a></li>
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<h4>What is SPACE-P?</h4>
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<p style="line-height:1.8"> Protein-protein interactions play a key role in biology. Designing and coordinating interactions in order to discover new drugs comes with a host of challenges. Our goal is to modify phage-assisted continuous evolution (PACE), specifically for protein interactions. PACE combines the bacteriophage M13 and <i>Escherichia coli</i> in a dynamic scheme whereby M13 only survives if it infects <i>E. coli</i>. This is achieved when the viral protein P3 is expressed. <b>SPACE-P</b> aims to incorporate a key-lock mechanism that regulates the expression of P3. In our model, the interaction between the protein HER2 and an affibody will be the key to open the lock. Over several phage life cycles, evolutionary pressure will favour the interactions with the greatest yield of P3, thereby increasing that phages virulence and the continued evolution of that particular affibody. Our method will reduce the time and cost of drug discovery and enable the interaction between many choose-able proteins. </p>
 
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Latest revision as of 23:35, 13 September 2015


Project

We have subdivided the Project section in seven different parts:

Abstract

Protein-protein interactions play a key role in biology. Designing and coordinating interactions in order to discover new drugs comes with a host of challenges. Our goal is to modify phage-assisted continuous evolution (PACE), specifically for protein interactions. PACE combines the bacteriophage M13 and Escherichia coli in a dynamic scheme whereby M13 only survives if it infects E. coli. This is achieved when the viral protein P3 is expressed. SPACE-P aims to incorporate a key-lock mechanism that regulates the expression of P3. In our model, the interaction between the protein HER2 and an affibody will be the key to open the lock. Over several phage life cycles, evolutionary pressure will favour the interactions with the greatest yield of P3, thereby increasing that phages virulence and the continued evolution of that particular affibody. Our method will reduce the time and cost of drug discovery and enable the interaction between many choose-able proteins.