Team:Yale

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<tr><td colspan="3"><div class = "well" ><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:10px"><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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Latest revision as of 03:37, 18 October 2014

Biosynthesis of an Anti-biofouling Surface Binding Polymer with the 21st Amino Acid- L-DOPA


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.

Main Campus:
Molecular, Cellular & Developmental Biology
219 Prospect Street
P.O. Box 208103
New Haven, CT 06520
Phone: 203.432.3783
igem@yale.edu
natalie.ma@yale.edu (Graduate Advisor)
Copyright (c) 2014 Yale IGEM