Dynamic Amino Acid Side-Chains Grafting on Folded Peptide Backbone

An efficient strategy for the synthesis of large libraries of conformationally defined peptides is reported, using dynamic combinatorial chemistry as a tool to graft amino acid side chains on a well-ordered 3D (3-dimension) peptide backbone. Combining rationally designed scaffolds with combinatorial side chains selection represents an alternative method to access peptide libraries for structures that are not genetically encodable. This method would allow a breakthrough for the discovery of protein mimetic for unconventional targets for which little is known.

Automated summary

This study reports an efficient strategy for synthesizing large libraries of peptides with defined conformations. The strategy involves using dynamic combinatorial chemistry to graft amino acid side chains onto a well-ordered 3D peptide backbone. By combining rationally designed scaffolds with combinatorial side chain selection, this method provides an alternative approach for accessing peptide libraries with structures that cannot be genetically encoded, thus enabling the discovery of protein mimetics for poorly understood targets.