471674 Expression and Isolation of a Precious Metal Binding Peptide Useful for Peptide-Directed Nanoparticle Synthesis

Monday, November 14, 2016
Grand Ballroom B (Hilton San Francisco Union Square)
Rita Tejada Vaprio1, Rudra Palash Mukherjee2, Lauren F. Greenlee3, Bob Beitle1 and Nicholas M. Bedford4, (1)Ralph E. Martin Department of Chemical Engineering, University of Arkansas, Fayetteville, AR, (2)REM Department of Chemical Engineering, University of Arkansas, Fayetteville, AR, (3)Ralph E. Martin Dept. of Chemical Engineering, University of Arkansas, Fayetteville, AR, (4)Applied Chemicals and Materials Division, Materials Measurement Laboratory, National Institute of Standards and Technology, Boulder, CO

The need for low-cost nanoparticle (NP) materials is of great importance within the context of new technologies for catalysis. Processes used today to produce peptide-directed NP morphologies are not scalable in an economical way primarily due to the challenges imposed by the use of a biological molecule. The purpose of this work is to address this challenge thorough the development of a cost effective means of peptide manufacturing.

The poster describes the cloning, fermentation, and isolation of a 45 amino acid long metal binding peptide, accompanied by an assessment of its ability to direct NP synthesis and morphology. A synthetic gene encoding a fusion protein of the metal binding peptide with Green Fluorescent Protein was constructed by overlap extension PCR, introduced into an arabinose inducible vector and transformed into Escherichia coli. High cell density fed batch culture was used to prepare extracts containing the fusion protein, with varying degrees of purity correlated to NP morphology. Finally, NP synthesis was characterized by electron microscopy.


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See more of this Session: Poster Session: Bioengineering
See more of this Group/Topical: Food, Pharmaceutical & Bioengineering Division