Dr Paul Leonard


+ Assistant Professor in Biomedical Sciences at Dublin City University (Sept. 17- present) and director of the Biomedical Innovations Group (BIG).
+ Serial entrepreneur, co-founder and CSO of Remedy Biologics Ltd.
+ Innovative and entrepreneurial research manager and technology inventor with 15 year’s post Ph.D. experience in academic and industrial research including lecturing and mentoring undergraduate and postgraduate students.
+  Previously, held a lectureship position (2009-2012) at Dublin City University lecturing in Biomedical Sciences at the School of Biotechnology and directed research as a Principal Investigator at the Biomedical Diagnostic Institute, Dublin City University, Ireland.
+  Previous director and head of R&D at Vaccinogen Ireland responsible for leading Vaccinogen’s overall strategy in Ireland including scientific, operational and financial. Responsible for business development, collaborations, funding diversity and tax incentives.
+  Experienced leading process improvements using Lean Six Sigma principles and building and managing multidisciplinary teams of research scientists in the areas of single cell analysis, vaccine development and manufacturing improvements, antibody engineering, high throughput screening, discovery and assay design. +  Demonstrated a proven publication and grant application record at DCU and received numerous invitations to contribute to international conferences and workshops in the US, Canada, China and Europe.
+  Lead inventor on granted and pending patents filed in the US and Europe.
+  Expert assessor (2012-present) for Innovate UK’s Biomedical Catalyst and Health and Life Sciences programmes, La Caixa’ (Spain) Life Sciences programmes (2018-present) and previous assessor for A-STAR.

Research Expertise

PhD Students

Select Publications

Measuring Antibody–Antigen Binding Kinetics Using Surface Plasmon Resonance
  Stephen Hearty, Paul Leonard, Richard O'Kennedy      2012      Methods in Molecular Biology

Surface plasmon resonance (SPR) is now widely embraced as a technology for monitoring a diverse range of protein-protein interactions and is considered almost de rigueur for characterizing antibody-antigen interactions. The technique obviates the need to label either of the interacting species and the binding event is visualized in real-time. Thus, it is ideally suited for screening crude, unpurified antibody samples that dominate early candidate panels following antibody selection campaigns. SPR returns both concentration and affinity data but when used correctly can also resolve the discrete component kinetic parameters (association and dissociation rate constants) of the affinity interaction. Herein, we outline some SPR-based generic antibody screening configurations and methodologies in the context of expediting data-rich ranking of candidate antibody panels and ensuring that antibodies with the optimal kinetic binding characteristics are reliably identified.


Developments in the production of biological and synthetic binders for immunoassay and sensor-based detection of small molecules
  Terry Fodey, Paul Leonard, John O’Mahony, Richard O’Kennedy, Martin Danaher      2011      Trends in Analytical Chemistry

The need for chemical and biological entities of predetermined selectivity and affinity towards target analytes is greater than ever, in applications such as environmental monitoring, bioterrorism detection and analysis of natural toxin contaminants in the food chain.

In this review, we focus on advances in the production of specific binders, in terms of both natural entities (e.g., antibodies) and synthetic binders (e.g., molecularly-imprinted polymers). We discuss the potential of emerging technologies for integration into immunoassay and sensing techniques. We place special emphasis on use of these technologies in bioanalytical applications.


Measuring Protein–Protein Interactions Using Biacore
  Paul Leonard, Stephen Hearty, Richard O'Kennedy      2011      Protein Chromatography: Methods and Protocols

The use of optical biosensors for studying macromolecular interactions is gaining increasing popularity. In one study, 1,179 papers that involved the application of biosensor data were identified for the year 2007 alone (Rich and Myszka, J Mol Recognit 21:355–400, 2008), the sheer volume and variety of which present a daunting task for the burgeoning biosensor user to accumulate and decipher. This chapter is designed to provide the reader with the tools necessary to prepare, design, and efficiently execute a kinetic experiment on Biacore. It is written to guide the Biacore user through basic theory, system maintenance, and assay set-up while also offering some practical tips that we find useful for Biacore-based studies. Many kinetic-based screening assays require rigorous sample preparation and purification prior to analysis. To highlight these procedures, this protocol describes the kinetic characterisation of single chain Fv (scFv) antibody fragments from crude bacterial lysates using an antibody affinity capture approach. Even though we specifically describe the capture of HA-tagged scFv antibody fragments to an anti-HA tag monoclonal antibody-immobilised surface prior to kinetic analysis, the same methodologies are universally applicable and can be used for practically any affinity pair and most Biacore systems. Key wordsAntibody–Surface plasmon resonance–Biacore–Kinetics–Biosensor analysis–Protein–protein interactions.


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