Matthew B. Francis
Chemist Faculty Scientist
The T.Z. and Irmgard Chu Distinguished Professor of Chemistry
Biography
Matt Francis is the Department of Chemistry Chair and the T.Z. and Irmgard Chu Distinguished Professor in Chemistry at UC Berkeley. Matt was born in Ohio and received his undergraduate degree in Chemistry from Miami University in Oxford, OH in 1994. From 1994-1999 he attended graduate school at Harvard University, working in the lab of Prof. Eric Jacobsen. His Ph.D. research involved the development of combinatorial strategies for the discovery and optimization of new transition metal catalysts. He then moved to UC Berkeley, where he was a Postdoctoral Fellow in the Miller Institute for Basic Research in Science. He worked under the guidance of Prof. Jean Fréchet, focusing on the development of DNA-based methods for the assembly of polymeric materials and the application of dendrimers for drug delivery. Matt started his independent career in the UC Berkeley Chemistry Department in 2001, and has built a research program involving the development of new organic reactions for protein modification. These new chemical tools have then been used to modify biomolecular assemblies to prepare new materials for diagnostic imaging, wastewater treatment, and solar cell development. For his research accomplishments, Matt has received the Dreyfus Foundation New Faculty Award, an NSF Career Award, a GlaxoSmithKline Young Investigator Award, the 2017 Bioconjugate Chemistry Lectureship Award from the American Chemical Society, and the 2019 Arthur C. Cope Scholar Award from the American Chemical Society. Matt became the chair of the chemistry department at UC Berkeley in 2018. Matt has also received the UC Berkeley Departmental Teaching Award on three occasions, the Noyce Prize for Excellence in Undergraduate Teaching, and the 2009 University Distinguished Teaching Award.
Research Interests
Research in the Francis group is focused on the development of new synthetic methods for the construction of nanoscale materials. The central strategy involves the attachment of new functional components to specific locations on structural proteins, and the subsequent self-assembly of these conjugates into new types of materials with useful electronic and biological functions.
Controlled Growth of Nanocrystalline Arrays Using Cytoskeletal Proteins
Modern synthetic methods for the preparation of inorganic nanocrystals have yielded promising new components for optical and electronic device construction. However, the organization of these materials into functional assemblies remains extremely difficult, in part because the small size of nanocrystals (2-10 nm) is well below the spatial resolution of most lithographic techniques. An alternative approach could be provided by attaching these nanocrystals to specific sites on the surfaces of fiber-forming cytoskeletal proteins, such as actin. By controlling the polymerization of the actin conjugates with additional proteins and small molecule natural products, specified locations could be connected with wire-like arrays of functional materials. Once constructed, the arrays could be converted into conductive linkages, thus providing an entirely new method for nanoscale circuit construction.
Modified Viral Capsids for the Assembly of Core/Shell Materials
A second research area involves the synthesis of three-dimensional nanostructures from the self-assembling proteins that form the outer coats of viruses. For example, by selectively modifying the top and bottom faces of the satellite panicum mosaic virus capsid protein, new types of core/shell materials could be obtained after assembly. These structures could be developed into particles capable of targeting desired tissue types and releasing their cargo of drug molecules. Functionalized viral capsids could also provide new tools for the investigation of multivalent binding interactions that occur in biological systems.
New Methods for Site-Selective Protein Modification
A central theme in this research program is the modification of structural proteins in specific locations in order to achieve homogeneous and predictable assembly. Site-directed mutagenesis provides a powerful set of tools for this purpose, and will be used extensively. However, there are limitations associated with this technique, and therefore the development of new chemical approaches for protein modification will be pursued as well. This research will take advantage of the rapidly expanding set of organic reactions that can proceed in aqueous solution, and will utilize asymmetric ligands and catalysts to enhance the selectivity of protein modifications. Combinatorial reaction libraries will play an important role in this research area.
