Document Type
Article
Publication Date
6-20-2023
Abstract
The late-stage functionalization of peptides and proteins holds significant promise for drug discovery and facilitates bioorthogonal chemistry. This selective functionalization leads to innovative advances in in vitro and in vivo biological research. It is a challenging endeavor to selectively target a certain amino acid or position in the presence of other residues containing reactive groups. Biocatalysis has emerged as a powerful tool for selective, efficient and economical modifications of molecules. Enzymes that have the ability to modify multiple complex substrates or selectively install nonnative handles have wide applications. Herein, we highlight enzymes with broad substrate tolerance that have been demonstrated to modify a specific amino acid residue in simple or complex peptides and/or proteins at late-stage. The different substrates accepted by these enzymes are mentioned together with the reported downstream bioorthogonal reactions that have benefited from the enzymatic selective modifications.
Recommended Citation
Alexander AK, Elshahawi SI. Promiscuous enzymes for residue-specific peptide and protein late-stage functionalization. ChemBioChem. 2023;24(17):e202300372. https://doi.org/10.1002/cbic.202300372
Copyright
Wiley
Included in
Amino Acids, Peptides, and Proteins Commons, Enzymes and Coenzymes Commons, Medicinal and Pharmaceutical Chemistry Commons, Other Pharmacy and Pharmaceutical Sciences Commons
Comments
This is the accepted version of the following article:
Alexander AK, Elshahawi SI. Promiscuous enzymes for residue-specific peptide and protein late-stage functionalization. ChemBioChem. 2023;24(17):e202300372. https://doi.org/10.1002/cbic.202300372
which has been published in final form at https://doi.org/10.1002/cbic.202300372. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.