Team:Yale

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<tr><td colspan="1"><div class = "well" ><p> <strong> Ariel Hernandez-leyva </strong> is a junior from Tinley Park, Illinois. He is majoring in Molecular, Cellular, and Developmental Biology. He has previously worked in the laboratory of Dr. Thomas Pollard in the MCDB department at Yale watching yeast divide in the warm, soothing darkness of the microscopy room. Outside of science he is interested in juggling and video games. His future plans include medical school and potential MD/PhD program. His back up plan involves Barnum and Bailey and a lot of face paint.</p></div></td>
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<tr><td colspan="1"><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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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-dopamine (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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Revision as of 23:38, 16 October 2014

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


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-dopamine (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