Experimental Oncology

Jack Tuszynski

Allard Chair & Professor
Experimental Oncology
Department of Oncology
University of Alberta
Cross Cancer Institute
11560 University Avenue
Edmonton, Alberta T6G 1Z2

Tel: 780.432.8906


Professor Jack Tuszynski received his M.Sc. with distinction in Physics from the University of Poznan (Poland) in 1980. He received his Ph.D. in Condensed Matter Physics from the University of Calgary in 1983. He did a Post-Doctoral Fellowship at the University of Calgary Chemistry Department in 1983. He was an Assistant Professor at the Department of Physics of the Memorial University of Newfoundland from 1983 to 1988, and at the University of Alberta Physics Department from 1988 to 1990, an Associate Professor from 1990 to 1993 and a Full Professor since 1993. He joined the Division of Experimental Oncology within the Cross Cancer Institute as the Allard Chair in 2005. He is on the editorial board of the Journal of Biological Physics, Journal of Biophysics and Structural Biology (JBSB), Quantum Biosystems, Research Letters in Physics, Water: a Multidisciplinary Research Journal and Interdisciplinary Sciences-Computational Life Sciences. He is an Associate Editor of The Frontiers Collection, Springer-Verlag, Heidelberg.
Research Interests
The major thrust of the computational biophysics group is in silico drug design for cancer chemotherapy applications and in vitro testing. Dr. Tuszynski’s research interests are strongly linked to the protein tubulin and the microtubules assembled from it. These have been studied using methods ranging from simple stochastic models to detailed molecular dynamics computer simulations, as well as through laboratory manipulations of living cells. Due to its prominent role played in eukaryotic cell division, tubulin is an important target for anti-cancer cytotoxic treatments. Our on-going research aim is to identify variants of known compounds showing greater tubulin isotype-specifc effects. These could potentially lead to more efficacious chemotherapy treatments with lower side effects. Other studies in our group have examined microtubule electrical, structural, and mechanical properties; proteins that bind to microtubules (MAPs); and the motor proteins in cells that travel along microtubules and actin filaments. We are also developing physiologically-based models and simulations for pharmacokinetic and pharmacodynamic applications.
  • Rational drug design
  • Microtubule assembly and function
  • Models of motor proten function
  • Integration of mathematical modelling into the pharmaceutical development process


Huzil, J. T., Mane, J., & Tuszynski, J. A. Computer assisted design of second-generation colchicine derivatives. Interdisciplinary Sciences: Computational Life Sciences (accepted 2009).
Demetrius, L., & Tuszynski, J. A. Quantum metabolism explains the allometric scaling of metabolic rates. Journal of The Royal Society Interface (accepted 7 August 2009).  View abstract
Barakat, K. H., Huzil, T. J., Luchko, T., Jordheim, L., Dumontet, C., & Tuszynski, J. A. (2009). Characterization of an inhibitory dynamic pharmacophore for the ERCC1-XPA interaction using a combined molecular dynamics and virtual screening approach. Journal of Molecular Graphics and Modelling 28(2), 113-130.  View abstract  
Mane, J. Y., Klobukowski, M., Huzil, T. J., & Tuszynski, J. A. (2008). Free energy calculations on the binding of colchicine and its derivatives with the a/β-tubulin isoforms. Journal of Chemical Information and Modeling 48(9), 1824-1832. View abstract
Gajewski, M., Tuszynski, J. A., Mori, H., Miyoshi, E., & Klobukowski, M. (2008). DFT studies of the electronic structure and geometry of 18-crown-6, hexaaza[18]annulene, and their complexes with cations of the heavier alkali and alkaline earth metals. Inorganica Chimica Acta 361(7), 2166-2171. View abstract
Freedman, H., Le, L., Tuszynski, J. A., & Truong, T. N. (2008). Determining solvation free energy changes with a hard-sphere reference by coupled Reference Interaction Site Model (RISM) simulation. Journal of Chemical Physics 112(8), 2340-2348. View abstract
Tuszynski, J. A., Craddock, T. J. A., & Carpenter, E. J. (2008). Bioferroelectricity at the nanoscale. Journal of Theoretical and Computational Nanoscience 5(10) 2022-2032. View abstract
Samarbakhsh, A., & Tuszynski, J. A. (2008). A “shooting bead” method for finding the cantilever stiffness and flexural rigidity of semiflexible rodlike biological filaments. Journal of Theoretical and Computational Nanoscience 5(10), 2041-2044. View abstract
Tuszynski, J. A., Malinski, W., Carpenter, E. J., Luchko, T. Huzil, J. T., & Ludueña, R. F. (2008). Tubulin electrostatics and isotype specific drug binding. Canadian Journal of Physics 86(4) 635-640. View abstract
Luchko, T. Huzil, J. T., Stepanova, M., & Tuszynski, J. A. (2008). Conformational analysis of the carboxy-terminal tails of human β-tubulin isotypes. Biophysical Journal 94(6), 1971-1982. View abstract
Rezania, V., Tuszynski, J. A., & Hendzel, M. (2007). Modeling transcription factor binding events to DNA using a random walker/jumper representation on a 1D/2D lattice with different affinity sites. Physical Biology 4(4), 256–267.  View abstract
Rezania, V., & Tuszynski, J. A. (2007). From a quantum mechanical description of the assembly process in microtubules to their semi-classical nonlinear dynamics. Quantum Biosystems 1(1), 1–20.
Shen, S., Hu, G., & Tuszynski, J. A. (2007). Analysis of protein three-dimensional structure using amino acid depths. The Protein Journal 26(3), 183–192. View abstract
Craddock, T. J. A., & Tuszynski, J. A. (2007). On the role of microtubules in the cognitive brain functions. NeuroQuantology 5(1), 32–57. View abstract
Huzil, J. T., Chen, K., Kurgan, L., & Tuszynski, J. A. (2007). The roles of β-tubulin mutations and isotype expression in acquired drug resistance. Cancer Informatics 3(15), 159-181.  View abstract
Fuite, J., Marsh, R. E., & Tuszynski, J. A. (2007). An application of Prony’s sum of exponentials method to pharmacokinetic data analysis. Communications in Computational Physics 2(1), 87–98.  View abstract