Functional Modification of Thioether Groups in Peptides, Polypeptides, and Proteins

Area of Science:

• Biochemistry
• Organic Chemistry
• Materials Science

Background:

• Proteins and peptides contain methionine (Met) and other thioether-containing amino acid residues.
• Modification of these residues offers unique chemical handles for functionalization.
• Existing methods primarily focus on cysteine modification.

Purpose of the Study:

• To review recent developments in the chemical modification of thioether-containing amino acids in peptides and proteins.
• To discuss the properties and potential applications of these modified biomolecules.
• To highlight the advantages and complementary nature of thioether modification compared to cysteine modification.

Main Methods:

• Review of literature on chemical modifications of methionine and other thioethers in peptides and proteins.
• Analysis of reported properties and applications of functionalized thioether-containing peptides and proteins.
• Comparison of thioether modification strategies with established cysteine modification techniques.

Main Results:

• Significant progress has been made in modifying natural Met residues.
• Emerging strategies involve incorporating new thioether-containing amino acids into peptidic materials.
• Functionalized products exhibit diverse properties and potential applications in various fields.
• Thioether modification provides a valuable alternative and complement to cysteine modification.

Conclusions:

• Chemical modification of thioether-containing amino acids is a rapidly advancing field.
• These modifications expand the toolkit for creating functionalized peptides and proteins.
• The versatility of thioether chemistry offers broad applicability in biochemistry, organic chemistry, and materials science.