Difference between revisions of "Team:UC Davis"

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<tr><td colspan="3"><div class = "well" style="margin-bottom:500px"><p> <strong><center>Producing a Novel Antimicrobial Surface-Binding Peptide Using an Improved T7 Expression System</center></strong><p>
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<tr><td colspan="3"><div class = "well" style="margin-bottom:50px"><p> <strong><center>Producing a Novel Antimicrobial Surface-Binding Peptide Using an Improved T7 Expression System</center></strong><p>
 
Biofilm formation on surfaces is an issue in the medical field, naval industry, and other areas. We developed an anti-fouling peptide with two modular components: a mussel adhesion protein (MAP) anchor and LL-37, an antimicrobial peptide. MAPs can selectively attach to metal and organic surfaces via L-3,5-dihydroxyphenylalanine (L-DOPA), a nonstandard amino acid that was incorporated using a genetically recoded organism (GRO).  Because this peptide is toxic to the GRO in which it is produced, we designed a better controlled inducible system that limits basal expression. This was achieved through a novel T7 riboregulation system that controls expression at both the transcriptional and translational levels.  This improved system is a precise synthetic switch for the expression of cytotoxic substances in the already robust T7 system. Lastly, the antimicrobial surface-binding peptide was assayed for functionality.  
 
Biofilm formation on surfaces is an issue in the medical field, naval industry, and other areas. We developed an anti-fouling peptide with two modular components: a mussel adhesion protein (MAP) anchor and LL-37, an antimicrobial peptide. MAPs can selectively attach to metal and organic surfaces via L-3,5-dihydroxyphenylalanine (L-DOPA), a nonstandard amino acid that was incorporated using a genetically recoded organism (GRO).  Because this peptide is toxic to the GRO in which it is produced, we designed a better controlled inducible system that limits basal expression. This was achieved through a novel T7 riboregulation system that controls expression at both the transcriptional and translational levels.  This improved system is a precise synthetic switch for the expression of cytotoxic substances in the already robust T7 system. Lastly, the antimicrobial surface-binding peptide was assayed for functionality.  
 
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<tr><td colspan="3"><a href="https://2014.igem.org/Team:Yale/Project"><img src="
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<tr><td colspan="3"><a href="https://2014.igem.org/Team:Yale/Notebook"><img src="https://static.igem.org/mediawiki/2014/2/2c/Yale_Notebook.png"  width="1100"></a></td></tr>
 
<tr><td colspan="3"><a href="https://2014.igem.org/Team:Yale/Notebook"><img src="https://static.igem.org/mediawiki/2014/2/2c/Yale_Notebook.png"  width="1100"></a></td></tr>
  
<tr><td colspan="3"><a href="https://2014.igem.org/Team:Yale/Achievements"><img src="https://static.igem.org/mediawiki/2014/2/29/Yale_Achivements.png"  width="1100"></a></td></tr>
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<tr><td colspan="3"><a href="https://2014.igem.org/Team:Yale/Achievements"><img src="http://www.blueoceanart.com/images/upload/AOP_KelpForest1_JimHellemn.jpg"  width="1100"></a></td></tr>
  
 
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Revision as of 09:30, 6 September 2015


Producing a Novel Antimicrobial Surface-Binding Peptide Using an Improved T7 Expression System

Biofilm formation on surfaces is an issue in the medical field, naval industry, and other areas. We developed an anti-fouling peptide with two modular components: a mussel adhesion protein (MAP) anchor and LL-37, an antimicrobial peptide. MAPs can selectively attach to metal and organic surfaces via L-3,5-dihydroxyphenylalanine (L-DOPA), a nonstandard amino acid that was incorporated using a genetically recoded organism (GRO). Because this peptide is toxic to the GRO in which it is produced, we designed a better controlled inducible system that limits basal expression. This was achieved through a novel T7 riboregulation system that controls expression at both the transcriptional and translational levels. This improved system is a precise synthetic switch for the expression of cytotoxic substances in the already robust T7 system. Lastly, the antimicrobial surface-binding peptide was assayed for functionality.