Charles Haynes

Contact Information
Michael Smith Laboratories
NEC #231, 2185 East Mall
Vancouver, BC, Canada, V6T 1Z4
Tel 1-604-822-5136
Fax 1-604-822-2114

Current Positions

  • Professor, Chemical and Biological Engineering, Applied Science
  • Professor, Michael Smith Laboratories, Science
  • Canada Research Chair in Interfacial Biotechnology

Research Interests

Purity and purification costs are becoming important issues in biotechnology as the industry matures and competitive products reach the marketplace. The primary objective of Dr. Haynes’ research is to develop new natural and recombinant-protein purification processes based on high-affinity interactions between target proteins or drugs and separation media. Fundamental research focuses on development of new instrumentation, particularly microcalorimetry and UV-resonance Raman spectroscopy, for quantifying the delicate energetics of biological interactions and binding. When engineered properly, molecular genetics techniques provide a robust method for purifying recombinant proteins from the complex aqueous solutions in which they are produced. Dr. Haynes, in collaboration with Drs. Kilburn and Warren of the Microbiology department, is interested in purification strategies which use the cellulose binding domains (CBD’s) of Cellulomonas fimi cellulases as affinity tags. Genetic or chemical linkage of a CBD to the target protein creates a fusion protein which binds strongly to cellulose and retains the biological activity of the fusion partner. Recovery of the target protein is then achieved through either a modest change in system variables or enzymatic cleavage of the polypeptide backbone at the protein/CBD linkage. Many protein purification processes rely on controlled and/or well characterized adsorption at solid-liquid or liquid-liquid interfaces. For instance, chromatographic separations, such as hydrophobic, displacement and ion-exchange chromatographies, are based on differences in binding affinities of proteins for the support material. Understanding protein adsorption at synthetic surfaces is also critical to the development of improved biomaterials for use in artificial organs, vascular grafts, haemodialysis cartridges, blood bags, etc. A second interest of Dr. Haynes concerns thermodynamic (including electrostatic) aspects of protein adsorption with the aim of revealing general principles and resolving the dominant forces governing adsorption processes. Synthesis of pharmaceutical drugs often requires precursors of specified chirality. However, chemical syntheses of drug precursors, such as amino acids, typically yield racemic mixtures. Dr. Haynes is involved in the development of large-scale, continuous processes for separating mixtures of chiral enantiomers. Research to date has involved the fabrication and characterization of ligands which selectively separate chiral therapeutics with a single hydrophilic chiral center.


  1. Huft J, Haynes CA, Hansen CL. Rapid Fabrication of High-Quality Microfluidic Solid Phase Chromatography Columns. Anal Chem. 2012 Dec 12.
  2. Ghosh P, Vahedipour K, Lin M, Vogel JH, Haynes CA, von Lieres E. Zonal rate model for axial and radial flow membrane chromatography. Part I: Knowledge transfer across operating conditions and scales. Biotechnol Bioeng. 2012 Oct 23.
  3. Francis P, von Lieres E, Haynes CA. Zonal rate model for stacked membrane chromatography. I: characterizing solute dispersion under flow-through conditions. J Chromatogr A. 2011 Aug 5;1218(31):5071-8.
  4. Hughesman CB, Turner RF, Haynes CA. Role of the heat capacity change in understanding and modeling melting thermodynamics of complementary duplexes containing standard and nucleobase-modified LNA. Biochemistry. 2011 Jun 14;50(23):5354-68.
  5. Singhal A, Haynes CA, Hansen CL. Microfluidic Measurement of Antibody-Antigen Binding Kinetics from Low-Abundance Samples and Single Cells.  Anal Chem. 2010 Sep 21.
  6. Kavoosi M, Creagh AL, Turner RF, Kilburn DG, Haynes CA. Direct measurement of the kinetics of CBM9 fusion-tag bioprocessing using luminescence resonance energy transfer. Biotechnol Prog. 2009 May-Jun;25(3):874-81.
  7. Francis P, Haynes CA.Scale-up of controlled-shear affinity filtration using computational fluid dynamics. Biotechnol J. 2009 May;4(5):665-73.
  8. Bordbar AK, Creagh AL, Mohammadi F, Haynes CA, Orvig C. Calorimetric studies of the interaction between the insulin-enhancing drug candidate bis(maltolato)oxovanadium(IV) (BMOV) and human serum apo-transferrin. J Inorg Biochem. 2009 Apr;103(4):643-7.
  9. Shaner RL, Allegood JC, Park H, Wang E, Kelly S, Haynes CA, Sullards MC, Merrill AH Jr. Quantitative analysis of sphingolipids for lipidomics using triple quadrupole and quadrupole linear ion trap mass spectrometers. J Lipid Res. 2009 Aug;50(8):1692-707.
  10. Coad BR, Kizhakkedathu JN, Haynes CA, Brooks DE. Synthesis of Novel Size Exclusion Chromatography Support by Surface Initiated Aqueous Atom Transfer Radical Polymerization” Langmuir, Web Release Date: 09-Oct (2007). DOI: 10.1021/la701703c
  11. Kavoosi M, Creagh AL, Kilburn DG, Haynes CA. Strategy for selecting and characterizing linker peptides for CBM9-tagged fusion proteins expressed in E. coli.  Biotechnol Bioeng., 98(3): 599-610 (2007).


  • Ph.D. University of California at Berkeley, 1991
  • B.Sc. University of Texas, Austin 1986