Abstract
AbstractHypervalent iodine compounds are powerful reagents for the development of novel transformations. As they exhibit low toxicity, high functional group tolerance, and stability in biocompatible media, they have been used for the functionalization of biomolecules. Herein, we report recent advances up to June 2021 in peptide and protein modification using hypervalent iodine reagents. Their use as group transfer or oxidizing reagents is discussed in this Minireview, including methods targeting polar, aromatic, or aliphatic amino acids and peptide termini.
Highlights
Peptides and proteins are increasingly considered as drug candidates by established pharmaceutical companies.[1]
Hypervalent iodine reagents have recently emerged as powerful tools for the functionalization of peptides and proteins
Many of them are known for their oxidizing character, while others have been used as electrophilic group transfer reagents
Summary
Peptides and proteins are increasingly considered as drug candidates by established pharmaceutical companies.[1] Around 80 peptide therapeutics are currently on the market, more than 150 peptides in clinical development, and 400–600 in preclinical studies.[1i] the need for novel bioconjugation strategies is constantly in demand to improve the properties of biomolecules or to study their biological function.[2] the number of chemical transformations suitable for effective peptide and protein functionalization is still limited They represent unique challenges for synthetic chemists, because of the range of functional groups present. They can react with nucleophilic and oxidizable amino acids and can be used for the development of new methods for biomolecule functionalization (Figure 1).[5]
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