Here, we describe a new technol., designed to accelerate peptide discovery by quick identification and optimization of the residues critical for protein-protein interactions or ligand binding.We called it PepFusion. It is based on ligation of short DNA sequences generated from known ligand-binding regions.We tested it by selecting peptide antagonists of interleukin-6 (IL-6), a key mediator of inflammatory diseases such as rheumatoid arthritis (RA), Crohn′s disease, and Castleman disease (CD).The PepFusion library demonstrated superiority over a random library by yielding a peptide with low micromolar affinity for IL-6, whereas the random library failed.The affinity of the peptide from the PepFusion library was further enhanced by addnl. rounds of mutagenesis leading to peptide variants with low nanomolar IL-6 affinity.In addition to generating highaffinity peptides, our method opens the way to solve the problem of the false pos. sequences, which are common with all display technologies.

A novel approach for selecting potent peptide inhibitors of the SARS-CoV2-Mpro protease

Author: Pisarchik, Alexander

AbstractHere, we describe a new high throughput selection technology for identifying exceedingly specific and effective peptide inhibitors. This technology incorporates the co-expression of a cytotoxic protein and a library of peptide variants inserted directly into a loop of a carrier protein. Selection is based on the cytotoxicity neutralization by a member of a peptide library binding to and inhibiting the cytotoxic protein. Our technology provides the flexibility of screening both cyclic and linear peptides. Herein, we demonstrate the power of this technology by developing selective inhibitors of the main coronavirus protease (Mpro) in a matter of weeks by screening libraries of cyclic and linear peptides. This technology opens up an opportunity to develop inhibitors for a wide range of previously undruggable targets.

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