Invited Speakers

Karsten Haupt is a Biochemist from the University of Leipzig, Germany. After obtaining a PhD in Bioengineering from Université de Technologie de Compiègne (UTC), France, he was a researcher at Lund University, Sweden and at INSERM, Paris, and an assistant professor at the University of Paris 12. Since 2003 he has been a full professor of Bioengineering at UTC, which is part of the Paris Sorbonne University Alliance, where he is the Head of the CNRS Laboratory for Enzyme and Cell Engineering. Karsten Haupt is a Senior Member of Institut Universitaire de France, and the co-founder of the companies PolyIntell (2004) and SensWay (2021). His present research interests include affinity technology, chemical sensors, synthetic antibodies (molecularly imprinted polymers), biomimetic polymers and nanomaterials for biomedical applications.

Presentation: Molecularly Imprinted Polymer Nanogels: Synthetic Peptide Antibodies for Biomedical Diagnostics and Therapy

Molecularly imprinted polymers (MIPs) [1] are synthetic antibodies that specifically recognize molecular targets. They are cross-linked polymers synthesized in the presence of a molecular template, which induces three-dimensional binding sites in the polymer that are complementary to the template in size, shape and chemical functionality. MIPs against proteins are obtained through a rational approach starting with in silico epitope design. Chemically synthesized peptide epitopes can then be used as templates in a solid-phase protocol for MIP synthesis [2]. Fluorescence binding assays, SPR and solution NMR (STD and WaterLOGSY) demonstrate that the MIP recognizes and binds its target with an affinity and selectivity like a biological antibody [3]. We demonstrate the potential of MIP nanogels (~50 nm) for diagnostics, bioimaging and medical therapy, on the example of cell surface protein targets [4], as well as soluble cytokines [5].

Bibliographical references

[1] Haupt, K., Medina Rangel, P.X., Tse Sum Bui, B. (2020) Chem. Rev. 120, 9554-9582.
[2] Tse Sum Bui, B., Mier, A., Haupt, K. (2023) Small 19, 2206453.
[3] Mier, A. et al. (2021) Angew. Chem. Int. Ed. 60 20849-20857.
[4] Medina Rangel, P.X. et al., (2020) Angew. Chem. Int. Ed. 59, 2816-2822.
[5] Herrera León, C. et al. (2023) Angew. Chem. Int. Ed. 62, e202306274.

Professor Emeritus Christopher R. Lowe, OBE, FREng was originally trained as a biochemist and following postdoctoral positions and a lectureship at the University of Southampton. He was appointed to the University of Cambridge in 1984 to  found the Institute of Biotechnology. He is a Fellow of  Trinity College, the Royal Academy of Engineering, the Institute of Physics and a Life Member of the Royal Institution.

The principal focus of his research programme has been the healthcare biotechnology sector, particularly in biologics, microbial technology and biosensors.  He has over 420 peer-reviewed publications, 8 books and monographs, >100 patents and has supervised 99 PhD students. He has won a number of National and International prizes. He has been the driving force for the establishment of 12 spin-out companies and has established two entrepreneurial Master’s courses: Bioscience Enterprise (MBE) in 2002 and Therapeutic Sciences (MTS) in 2018.

Presentation: Affinity Interactions: A 360° View of Past, Present and Future

Affinity interactions have been integral to the development of numerous underpinning applications in modern biotechnology. This talk will chart the various stages involved in the development of biological recognition and its exploitation from its early discovery events, through a semi-design and high throughput phase into a variety of applications in protein purification, enzyme immobilisation, biosensors, modified, truncated and catalytic antibodies and molecular imprinting. We are currently in a data-rich information age involving machine learning which is likely to transform native recognition systems into entirely novel highly selective ab initio designed affinity systems with applications well beyond biology.

Bibliographical references

A Biomimetic Protein G Affinity Adsorbent: An Ugi Ligand for Immunoglobulins and Fab fragments based on the Third IgG-Binding Domain of Protein G. G. El Khoury and C. R. Lowe (2013) J Mol Recognit. 26, 190-200.

Bespoke Affinity Ligands for the Purification of Therapeutic Proteins. G. El Khoury, B. Khogeer, C. Chen, K.H. Ng, S.I. Jacob and C.R. Lowe (2014) Pharmaceutical Bioprocessing 3, 139-152.

Affinity Ligands for Glycoprotein Purification based on the Multi-Component Ugi Reaction. C. Chen, G. El Khoury and C.R. Lowe (2014)J Chromatogr B Analyt Technol Biomed Sci 969, 171-180.

A Carbohydrate Ligand for the Specific Enrichment of Glycoproteins. C. Chen, G. El Khoury, P. Zhang, P.M. Rudd and C.R. Lowe (2016) J Chromatogr A 1444,8-20.

A Holographic Sensor based on a Biomimetic Affinity Ligand for the Detection of Cocaine. N.C.L. Oliveira, G. El Khoury, J.M. Versnel, G. Khalili Moghaddam, L.L. Sampaio, J. L. Lima-Filho and C.R. Lowe (2017) Sensors & Actuators B Chemical 27, 216-222.

Development and Application of Synthetic Affinity Ligands for the Purification of Ferritin-Based Influenza Antigens. S.I. Jacob, B. Khogeer, N. Bampos, T. Sheppard, R. Schwartz and C.R. Lowe (2017) Bioconjugate chemistry 28, 1931-1940.

Roger-Marc Nicoud, founder and CEO of Ypso-Facto, has forged a successful career as an entrepreneur in the life sciences industry. He holds a PhD in process simulation for the nuclear industry and founded Novasep in 1995 with the vision to develop comprehensive solutions for the production of bio- and synthetic molecules. As President and CEO during 20 years, he led the company's growth from 10 to 1,300 employees, with a EUR 300M turnover. In 2014, he founded Ypso-Facto as a service company offering assistance to industrial firms to develop, optimize and secure their chemical and bioprocesses. He wrote the book "Chromatographic Processes: Modeling, Simulation, and Design", Cambridge University Press, 2015.

Presentation: Considerations for designing Chromatographic processes based on a few decades of experience

Designing efficient process is a complex and fascinating task associating thermodynamic, kinetic and hydrodynamic contributions.
Typical questions are: "Should I use one or many columns?", "What is the impact of particle size?", "Is it better to inject a small, concentrated volume or a large diluted one?" and many others ...
The presentation will illustrate the fundamental concepts with different applications taken from bio-industry.

Bibliographical references

"Chromatographic Processes: Modeling, Simulation, and Design", Cambridge University Press, 2015 by Roger-Marc Nicoud

Presentation: Digital Twins towards Autonomous Manufacturing of Biopharmaceuticals

Richard Willson is Huffington-Woestemeyer Professor of Chemical & Biomolecular Engineering, Biology & Biochemistry, and Biomedical Engineering at the University of Houston, Faculty of Excellence at Tecnológico de Monterrey, and a Senior Affiliate of the Houston Methodist Hospital Research Institute.  He holds B.S. (honors) and M.S. degrees in Chemical Engineering from Caltech, and completed his Ph.D. in Biochemical Engineering and postdoctoral studies in Biochemistry at MIT. 

Dr. Willson is a recipient of the Presidential Young Investigator Award under the first Bush administration, an elected Fellow of the AIMBE, ACS, and AAAS, and a member of the US National Academy of Inventors. He was a founding member of the Technical Advisory Board of Moderna, and was formerly Associate VP for Technology Transfer of the University of Houston, at that time the public non-medical university with the largest patent royalty income in the USA.  His research interests are in the purification of biologics such as antibodies and mRNA vaccines, and the development of novel platforms for medical diagnostics and process analytical technology.

Presentation: What is protein A? Natural variation in IgG-binding proteins

Protein A of Staphylococcus aureus is used in most processes for purification of therapeutic antibodies. Current commercially-available protein A resins are based primarily on the sequence of protein A from the Cowan I strain of Staphylococcus aureus. There exist an extensive range of natural variation of protein A sequences, and a surprisingly large number of other IgG-binding proteins that are very distantly related to protein A but differ dramatically from it in sequence. There is no reason to believe that the protein A sequence selected by the pioneers in the field is the optimal choice for bioprocess applications. We have tested a range of alternatives and found human IgG-binding activity in proteins as little as 29 % identical to the sequence of the canonical Z domain of protein A. We are conducting biophysical characterization of these binders to elucidate their affinity for human IgG and IgGs from other species.