Protein quality and assay development for successful DNA-encoded library screening

Recorded On: 02/06/2018

Active hit identification from DNA-encoded library screens is driven by high quality protein targets. Because the effective concentration of individual DNA-encoded library molecules in the screen is very low, the immobilized protein target concentration must exceed the dissociation constant to drive protein-library molecule binding. The protein target should also be a consistent conformation and without aggregates so the resulting data is associated with a single protein form. Ensuring that the immobilized protein target maintains biochemical or biophysical activity in the course of selection biases the outcome to functionally active hits. In this presentation, case studies of protein target assessment enabling DNA-encoded library screening success will be shown. 

Allison Olszewski

X-Chem

Dr. Olszewski joined X-Chem in 2016 as Associate Director of Protein Biochemistry. She developed Avimer panning techniques against membrane-bound targets at Avidia, Inc. (acquired by Amgen in 2006) from 2006 to 2007. From 2007 to 2015 she worked at GlaxoSmithKline, where she expanded the use of DNA-encoded library technology to non-soluble targets. Before joining X-Chem, Dr. Olszewski managed the screening hit validation effort, and developed protein-protein interaction assays for the Small Molecule Assisted Receptor Targeting (SMART) technology platform at Warp Drive Bio. Dr. Olszewski received her B.S. in Biochemistry from the University of Delaware, and her Ph.D. in Organic Chemistry/Chemical Biology from the University of California, Irvine.

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