Chemical protein modification has become a valuable tool for developing modified proteins.
The complementary use of genetic and chemical approaches provides a large toolbox that allows the preparation of almost unlimited protein constructs from natural or synthetically modified residues.
This protein chemical diversity is usually achieved after translation, often referred to as post-translational protein modification (PTM), and is often responsible for much of the biodiversity found in nature.
These modifications include acylation, methylation, phosphorylation, sulfation, faranzylation, ubiquitination, and glycosylation, and play key roles in important cellular processes, including transport, differentiation, migration, and signaling.
Therefore, replicating this natural modification of a protein in an efficient and controlled manner (by introducing natural PTM) will provide an invaluable tool for studying its precise function.
In addition, the possibilities offered by introducing and (biological) orthogonal modifications of non-natural parts/amino acids (which usually improve the properties of natural PTM during isolation, analysis and processing) make site-selective modification of proteins a key tool for interrogation and intervention in in vitro and in vivo biological systems.Given the range of chemical modification methods available, it is now possible to decide which residues to target and which modifications to link to confer desired properties/functions (affinity probes, fluorophores, reaction tags, etc.).