Research

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Synthetic Proteins That Overcome Challenges to Small Molecule Drug Discovery

Researchers in the McNaughton lab integrate protein evolution, protein engineering, biochemistry and biophysics, and synthetic biology to identify, study, and inhibit disease-related protein-protein interactions — particularly those that present a substantial challenge to small molecule-centered drug discovery.

Modulating Disease-Relevant RNA Biochemistry 

Recent advances in RNA biochemistry have implicated a broad range of sequence diverse RNAs in human diseases. These structurally complex targets often frustrate therapeutic efforts centered on traditional small molecules (< 800 Da). In contrast, Nature has evolved a suite of proteins capable of highly specific and potent RNA targeting. These structural motifs are thus promising starting points for engineered or evolved RNA-binding proteins with enhanced affinity for disease-related RNAs, which may constitute a unique new class of protein therapeutics and basic research tools.    

Researchers in the McNaughton lab use biochemical methods and molecular evolution to identify and investigate new protein-RNA interactions. Such interactions may have therapeutic implications, as well as expand our understanding of design principles that facilitate sequence-selective RNA-protein interactions.

Methods for Intracellular Delivery of Protein Therapies and Imaging Reagents to Diseased Cells

Perhaps the most important impediment to their broader use is the difficulties associated with the potent delivery of these reagents across the lipid bilayer membrane of mammalian cells. 

Researchers in the McNaughton lab use protein evolution and engineering to identify new cell-selective protein transduction domains, and engineer new proteins that potently and selectively penetrate mammalian cells and access the cytosol.

Engineering and Evolving Synthetic Enzymes for Catalysis and High-Throughput Reaction Discovery

Researchers in the McNaughton lab use molecular engineering and high-throughput screening to identify new enzymes and metalloenzymes.


© McNaughton Lab, Colorado State University