Protein 2B4 is a natural killer (NK) cell activation receptor that can provide a co-stimulatory signal to other activation receptors. Based on recent studies, its signal transduction may be closely related to the phosphorylation of the immunoreceptor tyrosine-based switch motif (ITSM) sequence of the 2B4. As a result, protein chemical synthesis of 2B4 with phosphorylations is a pressing need to figure out 2B4’s mode of signal transduction. Our group developed the serine/threonine ligation (STL) and cysteine/penicillamine ligation (CPL), providing a strong
tool for the synthesis of peptides and proteins. However, the poor solubility of peptides brings a big challenge to the protein chemical synthesis, due to the difficulties of chemical ligation and purification steps. Herein, we developed a simple and general method to link the solubilizing tags via disulfide bond on resin, which is well compatible with STL and CPL and these solubilizing tags could be simply removed with desulfurization step in one pot. With our disulfide bond linked solubilizing tag method, the yields of peptides were remarkably increased and the reactivity of peptides during the serine/threonine ligation became better. Finally, we successfully synthesized the 2B4 tail and its different phosphorylation combinations for further investigation.  

Chemical Synthesis of Natural Killer Cell Receptor 2B4 Using Serine/Threonine Ligation Assisted with Disulfide Linked Removable Solubilizing Tag

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