Sulfation of tyrosine residues is an important post-translational modification that occurs on manysecretory as well as transmembrane proteins. It has been suggested that up to 1% of all tyrosine residues of the overall protein content in an organism are sulfated which makes this modification essential for numerous biological processes. However, one of the factors hindering the study of the significance of sulfotyrosine (sTyr) within a protein is the absence of a general method that enables the synthesis of sTyr peptides in satisfactory yields and purity.

Though employing the proper building blocks and optimizing the final cleavage protocol, we have successfully synthesized a lot of Tyr(SO3H) bearing peptides for research applications.