Justin Northrup
Head of R&D, ThirdLaw Molecular
Application of a 4.5 Billion Member DNA Encoded Library of Spiroligomer[TM] Macromolecules to Discover Low Nanomolar Binders for TNF-alpha
Company Description
Constrained peptides have garnered significant attention due to their potential to target proteins that are undruggable by small molecules. Innovations in this space will allow for targeting of challenging biological pathways, disrupting protein-protein interactions, and modulating immune responses. We have developed a highly advanced form of constrained peptide called Spiroligomer™ peptidomimetics – a class of synthetic peptidomimetics characterized by stable, spirocyclic structures which combine the versatility of peptides with preorganization that comes from their poly-cyclic fused-ring structure. The unique structure of Spiroligomer molecules provides them with several advantages over other approaches, including high affinity and specificity to a wide range of targets, immunity to proteolysis, and inherent cell permeability. We have synthesized a DNA encoded library (DEL) of 4.5 billion Spiroligomer™ macromolecules and screened it against more than a dozen proteins. From these initial screens, we have validated low nanomolar binding to multiple proteins of interest, including TNF-alpha and RCA-Lectin (a protein with ~85% homology to Ricin).
Bio
I'm the Head of R&D and Principal Scientist at ThirdLaw Molecular, having been with the company since it's founding in 2020. I received my BA in chemistry from Kalamazoo College in 2009, and I received my PhD in Organic Chemistry from Temple University in 2016, authoring numerous papers on the development of Spiroligomer molecules and their related chemistries. I moved on to a postdoc in chemical biology and radiochemistry with Dr. Mark Sellmyer in the Department of Radiology at the University of Pennsylvania. I've worked on Spiroligomer[TM] molecules since 2010.