In-Solution Affinity Measurement of a Drug-Induced Protein Complex

10 Jan, 2022 | Newsletters
In-Solution Affinity Measurement of a Drug-Induced Protein Complex
The ability to reduce the activity of the immune system in a controlled fashion represents one of the most important achievements in modern medicine.

Decades of research have led to a remarkable understanding of protein structure and function. However, proteins rarely act on their own and a quantitative understanding of their interaction mechanisms is key to the successful development of new drugs that enable the modulation of the cellular network of protein–protein interactions.    Using Microfluidic Diffusional Sizing (MDS) technology, we describe an in-solution assay to characterise the interaction of the immunosuppressive protein pair FKBP12 and mTOR induced by the small-molecule drug rapamycin.

This user guide describes microfluidic affinity antibody profiling (MAAP) against the SARS‑CoV‑2 S1 (K417N, E484K, N501Y, D614G) protein directly in serum samples.

The new Fluidity One-M system offers the latest technology for the purpose of quantifying and characterising protein interactions – even in complex backgrounds or with challenging targets, in a single experiment.

Fluidity One-M benefits: Uses microfluidic diffusional sizing (MDS) technology to measure changes in molecular size (hydrodynamic radius) as binding events occur Enables development of customised protocols to study a wide range of interactions – typical run time 35 minutes for 24 datapoints to determine KD Eliminates risk of binding artefacts or other surface constraints – measure directly in solution – no surface immobilisation Minimises consumption of precious samples – 3.5 μL per datapoint (application dependent), 50-80 μL to determine KD
Contact us for a demo
Request a quote now
Email us for more info