François Baneyx
Charles W. H. Matthaei Professor of Chemical Engineering
Adjunct Professor of Bioengineering
Acting Director UW Center for Nanotechnology
Site Director NSF National Nanotechnology Infrastructure Network
Co-Director NSF Genetically Engineered Materials Science and Engineering Center
Contact Information
| 307 Benson Box 351750 Seattle, WA 98195-1750 |
Phone: 206-685-7659 Fax: 206-685-3451 or 206-543-3778 E-mail: baneyx@u.washington.edu |
Education
Ingénieur, E.N.S.I.G.C., Toulouse (France), 1987.
Ph.D., University of Texas (Austin), 1991.
Postdoctoral Fellow, Du Pont (Wilmington), 1991.
For more information, please see the Baneyx Group Home Page
Research Interests
- Protein folding, protein engineering, protein expression
- Nanobiotechnology, molecular biomimetics
Biotechnology, Protein Technology, Nanobiotechnology
Research in the Baneyx laboratory lies at the intersection of engineering, biology and nanotechnology. Understanding how proteins fold into intricate three-dimensional shapes - or why they sometimes fail to do so - has far-reaching implications in medicine and biotechnology. Our group studies the genetics, regulation and structure-function relationship of a class of proteins that help other polypeptides reach a correct conformation. We investigate how these folding modulators can be used to facilitate the production of recombinant proteins and their connection with neurodegenerative diseases. In the nanobiotechnology arena, we are interested in isolating and characterizing short peptides that bind to inorganic or synthetic compounds. We engineer these peptides within well-characterized protein "scaffolds" and use the resulting designer proteins to nucleate, organize and assemble nanostructured materials exhibiting superior mechanical or opto-electronic properties.
Folding Modulators, Protein Folding and Protein Expression
Although the cloning of genes encoding proteins of commercial or therapeutic interest is now routine, the large-scale production of these polypeptides remains difficult owing to their propensity to misfold, aggregate or become toxic when expressed at high level in bacteria and other cells. Proteins are linear polymers of amino acids that must fold into a precise three-dimensional conformation to perform their function.
Ribbon structure of the Escherichia coli Hsp31 protein. This folding modulator is structurally homologous to human DJ-1, a protein implicated in early onset Parkinson's disease.
See PNAS 100:3137
While many small, single-domain proteins fold readily, more complex polypeptides (e.g., multidomain, disulfide-bonded and membrane proteins) require the assistance of folding modulators to reach a proper conformation or cellular location. These folding helpers, known as molecular chaperones, foldases and ushers, assist folding by stabilizing partially folded intermediates and/or catalyzing rate-limiting steps in the folding process. We are interested in understanding the regulation, function and mechanism of action of a variety of folding modulators and in determining how they interact with each other and with their substrates. By manipulating the intracellular concentration of molecular chaperones and foldases through genetic engineering, we seek to make the bacterium Escherichia coli an optimal host for the production of valuable recombinant proteins. Because folding modulators have been conserved through evolution and because many diseases are linked to protein misfolding, these studies also provide insights on the etiology of certain human diseases.
Nanobiotechnology and Molecular Biomimetics
Under thermodynamically unfavorable conditions, a Cu2O-binding peptide engineered within the DNA binding protein TraI drives the formation of 2 nm Cu2O particles surrounded by a protein core. When mixed with a circular DNA guide the core-shell particles assemble in the predicted geometry.
See JACS 127:15637
In display technologies, random sequences of amino acids exposed at the surface of a cell or a virus are screened and selected for their ability to bind to an immobilized protein or ligand. These techniques have long been used to map antibodies binding sites and to study protein-protein interactions. The same tools can be employed to isolate short polypeptides interacting with inorganic or synthetic materials of engineering interest. We are interested in isolating peptides that control the nucleation, growth rate, crystallography and morphology of inorganic materials and in understanding the fundamental rules that underpin protein-inorganic interactions. By engineering inorganic-binding peptides within the framework of functional protein "scaffolds", we seek to precisely control the positioning of inorganic and synthetic molecules to harness nanoscale effects (e.g., quantum confinement, field enhancement, improved mechanical properties.) and to assemble nanostructured materials of well-defined composition and geometry. We are also exploiting the ability of S-layer proteins to form crystalline arrays to grow inorganic "optical benches" onto which a variety of active molecules can be anchored. The resulting materials hold great promise for electronic, photonic, chemical and biosensing applications. These projects are carried out in collaboration with Dan Schwartz under the umbrella of the Genetically Engineered Materials Science and Engineering Center (GEMSEC), a NSF-MRSEC.
The S-layer of Sporosarcina ureae forms a square nanolattice. Electrodeposition can be used to grow various materials through the interstitial "holes" of the protein mask.
See Nano Letters 5:609
Selected Recent Publications
Sarikaya, M., C. Tamerler, A.K.-Y. Jen, K. Schulten and F. Baneyx, "Molecular biomimetics: nanotechnology through biology". Nature Mater., 2:577-585 (2003).
Quigley, P., K. Korotkov, F. Baneyx and W.G.J. Hol, "The 1.6 Å crystal structure of the class of chaperones represented by E. coli Hsp31 reveals a putative catalytic triad", Proc. Natl. Acad. Sci. USA, 100:3137-3142 (2003).
Baneyx, F. and M. Mujacic, "Recombinant protein folding and misfolding in Escherichia coli", Nature Biotechnol., 22:1399-1408 (2004).
Sastry, M.S.R., P. Quigley, W.G.J. Hol and F. Baneyx, "The linker-loop region of E. coli chaperone Hsp31 functions as a thermal gate that modulates high affinity substrate binding at elevated temperatures". Proc. Natl. Acad. Sci. USA 101:8587-8592 (2004).
Mujacic, M., M. Bader and F. Baneyx, "Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions". Mol. Microbiol., 51:849-859 (2004).
Thai, C.K., H. Dai, M.S.R. Sastry, M. Sarikaya, D.T. Schwartz and F. Baneyx, "Identification and characterization of Cu2O and ZnO binding polypeptides by Escherichia coli cell surface display: towards an understanding of metal oxide binding", Biotechnol. Bioeng. 87:129-137 (2004).
Dai, H., W.-S. Choe, C.K. Thai, M. Sarikaya, B. Traxler, F. Baneyx and D.T. Schwartz, "Nonequilibrium synthesis and assembly of hybrid inorganic-protein nanostructures using an engineered DNA-binding protein", J. Am. Chem. Soc. 127:15637-15643 (2005).
Allred, D.B., M. Sarikaya, F. Baneyx and D.T. Schwartz, "Electrochemical nanofabrication using crystalline protein masks". Nano Lett. 5:609-613 (2005).
Chow, I.-T.and F. Baneyx, "Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress", FEBS Lett. 579:4235-4241 (2005).
Chow, I.-T., M.E. Barnett, M. Zolkiewski and F. Baneyx, "The N-terminal domain of Escherichia coli ClpB enhances chaperone function", FEBS Lett. 579:4242-4248 (2005).
Shapiro, E., C. Lu and F. Baneyx, "A set of multicolored Photinus pyralis luciferase mutants for in vivo bioluminescence applications", Protein Eng. Des. Sel., 18:581-587 (2005).
Recent M.S. Theses
Recent Ph.D. Dissertations
