Peptide and protein engineering by modification of backbone and sidechain functional groups

Abstract

AbstractModifications of the sidechain and backbone of peptides and proteins are commonly used to improve their stability, to enhance their biological function, to enable and improve imaging and detection capabilities via conjugation to imaging agents and to otherwise introduce new properties. The most common approaches for modification and conjugation typically target amino acids such as lysine and cysteine. However, less abundant residues such as tyrosine, methionine and tryptophan are also potential targets for orthogonal modification. Non‐traditional modifications of common amino acids such as cysteine can also be used to introduce novel functional groups in a peptide sidechain. Additionally, modification via sortase is also very precise and site specific in biological conditions. This mini‐review article describes recent advances in selective modification reactions of peptides and proteins via these less common approaches. © 2021 Society of Industrial Chemistry.