Staff profile

I received my DSc. (Habilitation) from the Institute of Biochemistry and Biophysics, Polish Academy of Sciences, my Ph.D. in Biochemistry from the University of Leicester, and a B.Pharm (Hons) from the University of Nottingham, United Kingdom.

 

I carried out research at the John Innes Centre, UK and spent over a decade in Japan engaged in academic teaching and investigational research, and I was responsible for laboratories at Tokyo Institute of Technology, and RIKEN, Japan’s largest comprehensive scientific research institution.

 I served as an Extraordinary Professor at the Malopolska Centre of Biotechnology (MCB), at Jagiellonian University in Krakow, Poland. I have more than 20 years of experience in researching natural and artificial bionanomachines and have made significant contributions to the understanding of DNA gyrase an important antibacterial target, playing a major role in designing novel artificial structures from DNA and proteins including nanorobotic DNA boxes, protein nanotubes and protein cages. I am also a founder of nCage Therapeutics, a spinout from our academic work which is developing novel protein structures and therapeutics.

I was awarded the Leverhulme Trust International Professorship to set up the Centre for Programmable Biological Matter at Durham University. My group's research focus is on understanding and building natural and artificial biological nanomachines. We are interested in using biochemical, biophysical and structural biology tools to understand complex machine-like enzymes and use the same tools to investigate the function of artificial nanosystems which are built from protein, nucleic acid and lipid components.

Chapter in book

• Topogami: Catenating DNA Origami
  
  Wilkens, G., Stepien, P., Shaukat, A., & Heddle, J. (2025). Topogami: Catenating DNA Origami. In G. Zuccheri (Ed.), DNA Nanotechnology: Methods and Protocols (pp. 49-65). Humana. https://doi.org/10.1007/978-1-0716-4394-5_5
• Running rings around protein cages: a case study of artificial TRAP cages
  
  Gaweł, S., Naskalska, A., Osiński, N., & Gardiner Heddle, J. (2024). Running rings around protein cages: a case study of artificial TRAP cages. In M. Ryadnov & K. Matsuura (Eds.), Amino Acids, Peptides and Proteins: Volume 45 (pp. 45-63). Royal Society of Chemistry. https://doi.org/10.1039/bk9781839169328-00045

Journal Article

• Dynamic Assembly of Pentamer-Based Protein Nanotubes
  
  Koziej, L., Fatehi, F., Aleksejczuk, M., Byrne, M. J., Heddle, J. G., Twarock, R., & Azuma, Y. (2025). Dynamic Assembly of Pentamer-Based Protein Nanotubes. ACS Nano, 19(9), 8786–8798. https://doi.org/10.1021/acsnano.4c16192
• Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH‐Dependent Assembly
  
  Osiński, N., Majsterkiewicz, K., Pakosz-Stępień, Z., Azuma, Y., Biela, A. P., Gaweł, S., & Heddle, J. G. (2024). Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH‐Dependent Assembly. Macromolecular Rapid Communications. Advance online publication, Article 2400712. https://doi.org/10.1002/marc.202400712
• Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase
  
  Michalczyk, E., Pakosz-Stępień, Z., Liston, J. D., Gittins, O., Pabis, M., Heddle, J. G., & Ghilarov, D. (2024). Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase. Proceedings of the National Academy of Sciences, 121(49), Article e2407398121. https://doi.org/10.1073/pnas.2407398121
• A DNA Origami Bubble Blower for Liposome Production
  
  Wilkens, G. D., Stępień P., Sakai, Y., Islam, M. S., & Heddle, J. G. (2024). A DNA Origami Bubble Blower for Liposome Production. ACS Omega, 9(43), 43609–43615. https://doi.org/10.1021/acsomega.4c05297
• Reengineering of an Artificial Protein Cage for Efficient Packaging of Active Enzymes
  
  Azuma, Y., Gaweł, S., Pasternak, M., Woźnicka, O., Pyza, E., & Heddle, J. G. (2024). Reengineering of an Artificial Protein Cage for Efficient Packaging of Active Enzymes. Small. Advance online publication, Article 2312286. https://doi.org/10.1002/smll.202312286
• Virus-like particles derived from bacteriophage MS2 as antigen scaffolds and RNA protective shells
  
  Naskalska, A., & Heddle, J. G. (2024). Virus-like particles derived from bacteriophage MS2 as antigen scaffolds and RNA protective shells. Nanomedicine, 19(12), 1103-1115. https://doi.org/10.2217/nnm-2023-0362
• CRAFTing Delivery of Membrane Proteins into Protocells using Nanodiscs
  
  Stępień, P., Świątek, S., Robles, M. Y. Y., Markiewicz-Mizera, J., Balakrishnan, D., Inaba-Inoue, S., De Vries, A. H., Beis, K., Marrink, S. J., & Heddle, J. G. (2023). CRAFTing Delivery of Membrane Proteins into Protocells using Nanodiscs. ACS Applied Materials & Interfaces. Advance online publication. https://doi.org/10.1021/acsami.3c11894
• Production of Metallic Alloy Nanowires and Particles Templated Using Tomato Mosaic Virus (ToMV)
  
  Shah, S. N., Heddle, J. G., Evans, D. J., & Lomonossoff, G. P. (2023). Production of Metallic Alloy Nanowires and Particles Templated Using Tomato Mosaic Virus (ToMV). Nanomaterials, 13(19), Article 2705. https://doi.org/10.3390/nano13192705
• Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B
  
  Pakosz, Z., Lin, T.-Y., Michalczyk, E., Nagano, S., & Heddle, J. G. (2021). Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B. Antimicrobial Agents and Chemotherapy, 65(10). https://doi.org/10.1128/aac.00267-21
• Enzyme encapsulation by protein cages
  
  Chakraborti, S., Lin, T.-Y., Glatt, S., & Heddle, J. G. (2020). Enzyme encapsulation by protein cages. RSC Advances, 10(22), 13293-13301. https://doi.org/10.1039/c9ra10983h

Working Paper

• Structure ofEscherichia coliDNA gyrase with chirally wrapped DNA supports ratchet-and-pawl mechanism for an ATP-powered supercoiling motor
  
  Michalczyk, E., Pabiś, M., Heddle, J., & Ghilarov, D. (in press). Structure ofEscherichia coliDNA gyrase with chirally wrapped DNA supports ratchet-and-pawl mechanism for an ATP-powered supercoiling motor. bioRXiv. https://doi.org/10.1101/2024.04.12.589215