Knowledge and solutions for a changing world

François Baneyx

François Baneyx

 

 

 

 

 

 

Department Chair and Charles W.H. Matthaei Professor of Chemical Engineering

Adjunct Professor of Bioengineering

 

Office: 307 Benson

 

Phone: 206-685-7659
Fax: 206-685-3451 or 206-543-3778

Education

  • Ingénieur, E.N.S.I.G.C., Toulouse (France), 1987.
  • Ph.D., University of Texas (Austin), 1991.
  • Postdoctoral Fellow, Du Pont (Wilmington), 1991.

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.
 

Protein ribbon
 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, molecular biomimetics

 
Peptide
 
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.
 

 
nanolattice
 
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
 

Recent Publications

 
  • Sedlak, R.H., Hnilova, M., Grosh, C., Fong, H., Baneyx, F., Schwartz, D.T., Sarikaya, M., Tamerler, C., Traxler, B. 2011. Engineering Escherichia coli Silver-Binding Periplasmic Protein That Promotes Silver Tolerence. Applied And Environmental Microbiology 2012, 78(7), pp. 2289-2296.
  • Baneyx, F. 2012. A ribosomal surprise. Biotechnology Journal 2012, 7(3), pp. 326-27.
  • Chiu, D., Zhou, W.B., Kitayaporn, S., Schwartz, D.T., Murali-Krishna, K., Kavanagh, T.J., Baneyx, F.  Biomineralization and Size Control of Stable Calcium Phosphate Core-Protein Shell Nanoparticles: Potential for Vaccine Applications. Bioconjugate Chemistry 2012, 23(3), pp. 610-617.
  • Nannenga, B.L., Baneyx, F. Enhanced expression of membrane proteins in E. coli with a P-BAD promoter mutant: synergies with chaperone engineering strategies. Microbial Cell Factories 2011, 10(Article #105).
  • Zhou, Weibin, Baneyx, F. Aqueous, Protein-Driven Synthesis of Transition Metal-Doped ZnS Immuno-Quantum Dots. ACS Nano 2011, 5(10), pp. 8013-8018.
  • Baneyx, F., Nannenga, B.L. CHAPERONES: A story of thrift unfolds. Nature Chemical Biology 2010, 6(12), pp. 880-881.
  • Puertas, J.M., Nannenga, B.L., Dornfeld, K.T., Betton, J.M., Baneyx, F. Enhancing the secretory yields of leech carboxypeptidase inhibitor in Escherichia coli: influence of trigger factor and signal recognition particle. Protein Express Purif 2010, 74, pp.122-128.
  • Zhou, W., Schwartz, D.T., Baneyx, F. Single-pot biofabrication of zinc sulfide immuno-quantum dots. J. Am. Chem. Soc. 2010, 132, pp. 4731-4738.
  • Kitayaporn, S., Hoo, J.H., Böhringer, K., Baneyx, F., Schwartz, D.T. Orchestrated structure evolution: accelerating direct-write nanomanufacturing by combining top-down patterning with bottom-up growth. Nanotechnology 2010, 21, 195306 (7pp).
  • Grosh, C., Schwartz, D.T., Baneyx, F. Protein-based control of silver growth habit using electrochemical deposition. Cryst. Growth Des. 2009, 9, pp. 4401-4406.
 
 

Contact Us

Dept. of Chemical Engineering

phone: (206) 543-2250
fax: (206) 543-3778

dand@cheme.washington.edu