On-Demand Webinar: Characterizing binding interaction between PD-1/PD-L1 directly from cell lysates using MST
The involvement of the immune system in tumor control is becoming well understood. The tumor environment is in a state of equilibrium between the elimination of cancer cells by the immune system and their proliferation. The immuno-evasion mechanisms that allow tumor cells to remain in equilibrium with the host depends on the overexpression of immunoregulatory molecules such as PD-L1 and its interaction with PD-1 expressed on tumor-infiltrating T lymphocytes. Blocking this interaction is being considered as a more targeted therapeutic approach that blocks the interaction of PD-1 with its ligands, leading to various clinical trial using monoclonal antibodies anti-PD-1 or anti-PD-L1 in several types of cancers. In order to develop such therapies, it is imperative to characterize the interaction between PD-1 and PD-L1. In this webinar we will show how we employed MicroScale Thermophoresis (MST) for the quantitative analysis of the binding affinity between these two molecules. Particularly we describe a method that utilizes low sample consumption and no tedious purification step of the protein of interest.
About the speaker
IRCL (Institut pour la Recherche sur le Cancer de Lille)
I graduated from the University of Bordeaux with a master’s degree in organic chemistry with a specialization in medicinal chemistry. I then decided to get deeply into drug design as I graduated from the ENSCL in this field with a one-year specialized master’s degree. Following my Internship in the UMR-S 1172, my aim was to develop microscale thermophoresis applied to the PD-1/PD-L1 pathway. We opted for a purification-free protocol inspired by previous work lead on GFP-fused proteins. I was then recruited as Engineer to continue this work and to screen small molecules targeting PD-1 or PD-L1 using MST, SPR, and FRET assays. I am currently working on a lot of protein-protein interaction projects involving MST.