Antimicrobial Adhesive Peptide Synthesis with an Improved T7 Expression System

Biofilm formation is a deleterious process in the medical and shipping industries. Protein adsorption, cell-adhesion, and subsequent biofilm formation have been found to lead to failure of medical implants and infection in patients. Government and industry spend upwards of $5.7 billion annually in the control of marine biofouling. High levels of biofouling result in increased drag and the subsequent loss of hydrodynamic performance. However, concerns of environmental toxicity often arise in materials being investigated as antibiofouling such as copper paints and Muntz metal. Therefore, we set out to develop a biomimetic antifouling coating. Mussels are notoriously capable of forming high strength coordination and covalent bonds with inorganic and organic surfaces. The primary modality of adhesion is through the secretion of L-dopamine (L-DOPA) containing mussel foot proteins (mfp). Using the adhesion capabilities of mfp’s, we decided to design a strain of E. coli that could synthesize a recombinant mfp tagged linked to an antimicrobial peptide. Our project involved the design of a tightly regulated mechanism of synthesis of this antimicrobial adhesive peptide. We aim to test the functionality of our peptide with biofouling and adhesion assays using an original rig to introduce liquid based erosion on treated surfaces.


  • Presented at iGEM Grand Jamboree (note no Regional Jamborees held in 2014) in Manufacturing Category
  • Oral and Poster Presentation
  • Bronze Medal


  • Two of our researchers, Alexandru Buhimschi and Ariel Hernandez-Leyva, are working on finalizing the summer work for publication in a peer-reviewed journal. 

For more information about the project, please visit our 2014 wiki!