Exploring the Solid-Phase Synthesis of ­Sulfotyrosine Peptides

• Published in: European journal of organic chemistry Vol. 2015; no. 34; pp. 7413 - 7425
• Main Authors: Vale, Nuno, Carvalho Veloso, Rita, Gomes, Paula
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01.12.2015; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Chemical industry; Peptides; Post-translational modifications; Protecting groups; Protein modifications; Proteins; Solid-phase synthesis; Sulfopeptides
• ISSN: 1434-193X; 1099-0690
• DOI: 10.1002/ejoc.201500715

Tyrosine sulfation is a common post‐translational modification operative in many biological processes, including hemostasis and intracellular trafficking. However, the precise structural and functional role of sulfotyrosine residues is not fully understood, so there is a demand for further detailed studies on the role of tyrosine sulfation in biochemical processes. Unfortunately, studies on the biological roles of tyrosine sulfation are hampered by difficulties in gaining access to large quantities of high‐purity and homogeneous sulfoproteins and sulfopeptides. This, however, may be addressed by appropriate solid‐phase peptide synthesis strategies, and these constitute the core subject of this review. An overview of efficient approaches to the synthesis of sulfopeptides and their associated pros and cons is presented. The structural and functional role of sulfotyrosine residues is not fully understood because is difficult to gain access to large quantities of high‐purity and homogeneous sulfopeptides. Efficient approaches to the synthesis of sulfopeptides can be developed by appropriate solid‐phase phase peptide synthesis strategies, the principal subject of this review.