This project seeks to enable traditional organic chemical transformations particularly in organic solvents on large proteins. Our strategy is to utilize a biomimetic mineralization process to coat the entirety of the tobacco mosaic virus (TMV) in the porous confines of a coordination polymer. I will present my project toward extending this work into the modification of exposed amino acids on TMV to attach small molecules that would otherwise be insoluble in the traditional aqueous media normally required for such transformations.<br/>TMV is a helical tube-shaped plant virus consisting of 2130 identical coat proteins spiraled around a single strand of viral RNA. The virus is 300 nm long, 18 nm in diameter, and has a 4 nm pore lengthwise down the middle of the tube. TMV can be disassembled and reassembled in physiological (aqueous) conditions, and it is stable under a wide range of pH and temperatures. TMV coat proteins have exposed tyrosine and glutamate residues that may be exploited for bioconjugation, allowing TMV to act as a scaffold for building larger macromolecules.<br/>This project seeks to coat TMV with a hydrolytically stable crystalline coordination polymer in order to provide stability in a wide range of solvents that TMV cannot normally withstand. While embedded in the crystals, the exposed tyrosine and glutamate residues are still exposed, as reactants are able to diffuse through the pores and react with the TMV outer surface. These bioconjugation reactions will now be able to be performed in normally denaturing organic solvents, something not done before.

Tobacco mosaic virus stabilized by coordination polymers

251st National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.