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

26 Oct, 2021 | Newsletters
In-Solution Affinity Measurement of a Drug-Induced Protein Complex
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.  
In the study presented here we have quantified the effect of rapamycin, a small molecule immunosuppression drug, on the protein complex formation of FKBP12 and mTOR using an in-solution assay that enables the characterization of otherwise challenging multi-protein complexes under close to native conditions.  

This collection of must-watch webinars cover a range of topics from measuring antibody affinity in serum to monitoring of SMALP nanodisc formation, to quantifying the stoichiometry and binding affinity of protein–protein interactions in complex backgrounds.  All webinars are available to view on demand  

Immune responses to SARS-CoV-2
In this webinar, Professor Akiko Iwasaki will discuss immune responses in COVID-19 patients with moderate and severe disease. She will compare viral load, immune phenotype and cytokines that are predictive of mortality, and discuss signatures of cytokines and growth factors that associate with recovery vs. disease exacerbation.

Safe, Rapid and Variant-Specific Affinity-Based Virus-Neutralization Assays
A new type of rapid assay is discussed based on quantifying protein interactions and provides functional insights equivalent to the gold standard cell-based neutralization assay by measuring the affinity, concentration, and neutralization potential of antibodies against the SARS-CoV-2 spike protein directly in serum. 

Take a closer look: Fluidity One-W Serum highlights
* Uses microfluidic diffusional sizing (MDS) technology to measure changes in molecular size (hydrodynamic radius) as binding events occur
* Enables development of customized protocols to study a wide range of interactions – typical run time 8-14 minutes per datapoint
* Eliminates risk of binding artefacts or other surface constraints – measure directly in solution – no surface immobilization
* Minimizes consumption of precious samples – 5 μL per datapoint, 60-100 μL to determine KD
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