Binding assays are the primary windows for elucidating protein interactions associated with cancer and are crucial for screening candidate drugs. However, the need to work with purified proteins is a substantial bottleneck of these assays. Technologies that measure binding affinities directly on cell lysates offer a unique opportunity to quantify binding interactions in near in vivo conditions, providing additional information on the efficacies of the binding events. And on the practical side, it saves researchers time and money.
Cancer can evade the immune system by tricking T cells into exhaustion — a state of ineffective activity that prevents them from killing the tumor.
To achieve this, cancer cells express PD-L1, a protein that delivers the ‘do not attack’ signal once bound to its receptor PD-1 on T cells. Because inhibition of this interaction reverses T cell exhaustion and reduces tumor progression, there’s great interest in finding stronger and more specific inhibitors in an easier and faster way.
In this webinar you will learn how:
- MST makes it possible to quantify the binding affinity between PD-L1 and PD-1 directly in whole cell lysates
- The Kd calculated by MST confirmed that PDL-1 and PD-1 interact at a much higher Kd than previously reported
- A fragment-based approach uses MST to find other small PD-L1 inhibitors for potential therapeutic applications
To learn more about how to perform binding assays with MST directly on cell lysates, watch the full on-demand webinar.
