Sulfation of the amino acid residues of proteins is a significant post-translational modification, the functions of which are yet to be fully understood. Current sulfation methods are limited mainly to O-tyrosine (sY), which requires negatively charged species around the desired amino acid residue and a specific sulfotransferase enzyme. Alternatively, for solid-phase peptide synthesis, a de novo protected sY is required. Therefore, synthetic routes that go beyond O-sulfation are required. We have developed a novel route to N-sulfamation and can dial-in/out O-sulfation (without S-sulfurothiolation), mimicking the initiation step of the ping-pong sulfation mechanism identified in structural biology. This rapid, low-temperature and non-racemising method is applicable to a range of amines, amides, amino acids, and peptide sequences.

中文翻译：

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小分子，氨基酸和肽的N-和O-硫酸化的化学方法。

蛋白质氨基酸残基的硫酸化是重要的翻译后修饰，其功能尚待充分了解。当前的硫酸化方法主要限于O-酪氨酸（sY），其需要在期望的氨基酸残基和特定的磺基转移酶周围带负电荷的物质。或者，对于固相肽合成，需要从头保护的sY。因此，需要超越O-硫酸化的合成途径。我们已经开发出一种新的途径来进行N-磺化反应，并且可以拨入/拨出O-硫酸化反应（不进行S-硫代硫代硫酸化反应），从而模仿了结构生物学中确定的乒乓硫酸化机制的起始步骤。这种快速，低温且非消旋的方法适用于一系列胺，酰胺，氨基酸和肽序列。