Workshops will be held on Nov. 8, 2020 before conference start. Register for the workshops during the registration procedure following Link.
Cristina Peixoto (iBET, Portugal)
8.11.2020, 11:45 – 13:15
Biotherapeutic particles are playing an increasingly important role in the different fields of vaccination, gene therapy, and cancer treatment. Virus-based biopharmaceuticals are examples of these very large and complex molecules that have been successfully applied in these different areas. Although these particles are different, they present some similarities besides their size range and challenges regarding the biomanufacturing and translation to the clinic. This workshop will provide insights on virus purification using examples and shared experiences. It will cover main operation units, technologies, process development and quality considerations.
Alois Jungbauer (BOKU, Austria) and Cristina Cabral (University of Beira Interior, Portugal)
8.11.2020, 13:30 – 15:00
The request for mechanistic understanding of processes has completely changed the paradigm of process development and process validation in biopharmaceutical manufacturing. For chromatographic separation processes the equilibrium binding conditions, also referred to as adsorption isotherms, are important to get a theoretical understanding on the maximum possible binding capacity and are the basis for mathematical description of the separation processes. In this pre-conference workshop we will provide the theoretical basis and the state-of-the-art in experimental approaches to monitor biomolecule – surface interactions in order to better understand equilibrium binding conditions. The participants will be offered an overview of different techniques: conventional adsorption measurements with finite and infinite bath, fluorescence assays, Attenuated Total Reflectance Infrared Spectroscopy (ATR-FTIR), Differential Scanning Calorimetry (DSC), Isothermal Titration Calorimetry (ITC), Flow Microcalorimetry (FMC) and Small Angle X-ray scattering (SAX). Specific advantages and drawbacks for each of the techniques to shed light on biomolecule mechanism of adsorption will be discussed. Focus will be put on FMC and SAX, as two non-labeling techniques capable of simulating a dynamic chromatography system allowing online and in situ monitoring of the adsorptive process. Finally, we will cover present applications of these in situ monitoring techniques to better understand antibodies separation by affinity chromatography with protein A, hydrophobic interaction chromatography and ion-exchange chromatography highlighting current challenges as well as future opportunities.
Sophia Hober (KTH, Sweden) and Michel Eppink (Synthon, The Netherlands)
8.11.2020, 15:15 – 16:45
Molecular interactions, and more specifically biomolecular interactions, are studied and measured in order to predict behaviour in living systems. In medical and pharmaceutical studies, the interaction of e.g. two proteins with each other is of importance to be able to predict the events in a human body. Many techniques to study protein-protein interactions exist, all with their own advantages and drawbacks. Surface plasmon resonance (SPR) has become one of the most widely applied techniques ever since the availability of the first commercial instruments in the 1990s. With this technology, protein-protein interactions are measured in real-time and essentially label-free [1,2]. Within the area of biotechnology SPR is commonly used both to assess potential therapeutics that bind certain target molecules and to develop new and specific purification and diagnostic tools. Due to the recently established protein selection strategies that open up the possibility of customized binders, this type of binders is increasing both in numbers and usability. Within this workshop we will discuss different strategies for development and characterization of binders for various purposes.
 de Mol, N. J. and Fischer, M. J. Surface plasmon resonance: a general introduction. Methods Mol.Biol. 2010; 627 1-14
 Willander, M. and Al-Hilli, S. Analysis of biomolecules using surface plasmons. Methods Mol.Biol. 2009; 544 201-229
Figure: Principle of surface plasmon resonance