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The Francis group is interested in the design of new materials by protein modification. In order to tackle a large engineering project on proteins, and in particular designing in multiple orthogonal functions onto a single scaffold, the group also devotes a great deal of it's effort toward the creation of new site-selective protein modifications. Our work then focuses on two areas of development: Methodology and Materials.
Our methodology work primarily targets native amino acid residues. Thusfar, we have developed new native modifications of Tyrosine, by alkylation and a Mannich-Type coupling, Tryptophan, by using rhodium carbenoids, the N-Terminus of proteins, and amines, by reductive amination.
Our groups Materials projects employ existing and new modifications of protein sidechains as a means of building up scaffolds for projects that require, or benefit from, site-selective, spatially arranged function. Our work has shown that intact viral capsids can be transferred to organic solvent, and that the spherical viral capsid MS2 can possibly be used as a drug delivery unit.