Tryptophan-specific modification and diversification of peptides and proteins

Area of Science:

• Biochemistry
• Chemical Biology
• Proteomics

Background:

• Tryptophan is present in 90% of proteins, despite being the second-least abundant amino acid.
• Chemoselective functionalization of tryptophan allows for site-specific modification of proteins.
• Bioconjugated proteins and peptides are increasingly important as therapeutic agents.

Purpose of the Study:

• To provide a comprehensive review of recent advances in tryptophan-specific modification and diversification of peptides and proteins.
• To highlight the significant applications of these modified biomolecules.
• To identify literature gaps and future opportunities in the field.

Main Methods:

• This review synthesizes recent literature on tryptophan-specific chemical modifications.
• It covers methods for peptide and protein diversification.
• The focus is on strategies enabling site-selective bioconjugation.

Main Results:

• Recent advances have significantly expanded the toolkit for tryptophan-specific protein modification.
• These methods facilitate site-selective bioconjugation, enabling precise control over protein structure and function.
• Applications span proteomics, protein engineering, cell imaging, and drug discovery.

Conclusions:

• Tryptophan modification is a powerful strategy for creating functional protein and peptide bioconjugates.
• The field offers numerous opportunities for innovation in biomolecular design and application.
• Further research can enhance the utility of these methods in various biological and medical contexts.