Homogeneous Sulfopeptides and Sulfoproteins: Synthetic Approaches and Applications To Characterize the Effects of Tyrosine Sulfation on Biochemical Function

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• 作者：Martin J. Stone ; Richard J. Payne
• 刊名：Accounts of Chemical Research
• 出版年：2015
• 出版时间：August 18, 2015
• 年：2015
• 卷：48
• 期：8
• 页码：2251-2261
• 全文大小：657K
• ISSN：1520-4898

文摘

Post-translational modification of proteins plays critical roles in regulating structure, stability, localization, and function. Sulfation of the phenolic side chain of tyrosine residues to form sulfotyrosine (sTyr) is a widespread modification of extracellular and integral membrane proteins, influencing the activities of these proteins in cellular adhesion, blood clotting, inflammatory responses, and pathogen infection. Tyrosine sulfation commonly occurs in sequences containing clusters of tyrosine residues and is incomplete at each site, resulting in heterogeneous mixtures of sulfoforms. Purification of individual sulfoforms is typically impractical. Therefore, the most promising approach to elucidate the influence of sulfation at each site is to prepare homogeneously sulfated proteins (or peptides) synthetically. This Account describes our recent progress in both development of such synthetic approaches and application of the resulting sulfopeptides and sulfoproteins to characterize the functional consequences of tyrosine sulfation.