Marcel Passon

Marcel Passon

 

 

 

 

 

Contact

Marcel Passon
Laboratory for General Biochemistry and Physical Pharmacy
Ghent University
Ottergemsesteenweg 460
9000 Gent
Belgium
Tel: 0032 9 264 8047 (secretary)
Tel: 0032 9 264 8049 (direct)

E-mail: Marcel.Passon@UGent.be

Biography

Marcel Passon started his Bachelor in Pharmaceutical Sciences at LMU Munich in 2014. In 2019, he obtained his Master’s Degree and in 2021, he became a licensed pharmacist in Germany. He performed his master thesis, titled ‘Impact of Disease-Causing Missense Mutations on Subcellular Localization and Function of the CLN3 Protein’ at the Walther Straub Institute of Pharmacology and Toxicology at the Medical Faculty of LMU Munich. In February 2022, he joined the Laboratory of General Biochemistry and Physical Pharmacy at Ghent University as a PhD student in the new research group of Prof. Dr. Hristo Svilenov.

Research interests

Antibody engineering, biopharmaceutics, biophysical characterization of proteins, formulation development of biologics

Summary of Research Project(s)

Immunoglobulin G (IgG) antibodies are essential for the therapy of severe diseases. However, not all IgGs that bind to pharmacological targets can become drugs. Therapeutic antibody candidates should also exhibit favourable (drug-like) physicochemical properties like high thermal stability.
Conventional IgGs use up to six hypervariable loops called complementarity-determining regions (CDRs) to bind antigens. The CDR composition has a large impact on the drug-like properties. It was recently discovered that, in contrast to conventional antibodies, some bovine antibodies bind to antigens via a knob mini-domain located in one ultra-long CDR. The aim of this project is to systematically study the biophysical properties of antibodies containing different knob mini-domains in their ultra-long CDRs. I will achieve my aim by (i) studying the effect of different knob minidomains on the drug-like physicochemical properties of bovine antibodies, (ii) developing universal human antibody scaffolds as an acceptor of knob mini-domains, and (iii) assessing how the grafting of different knob mini-domains affects the properties of the universal human antibody scaffolds. The project outcome will be a better understanding of the biophysical properties and stability of antibodies with ultra-long CDRs that can potentially lead to a new platform approach for the straightforward development of novel therapeutic IgGs.