Chemical synthesis of native S‐palmitoylated membrane proteins through removable‐backbone‐modification‐assisted Ser/Thr ligation
Résumé
Preparation of native S-palmitoylated (S-palm) membrane proteins represents one of the unsolved challenges in chemical protein synthesis. Herein, we reported the first chemical synthesis of S-palm membrane proteins by reversible backbone modification assisted Ser/Thr Ligation (RBM$^{GABA}$ -assisted STL). This method involves two critical steps: (1) Synthesis of S-palm peptides by a new γ-aminobutyric acid group-based RBM (RBM$^{GABA}$) strategy, (2) Ligation of the S-palm RBM-modified peptides to give the desired S-palm product by STL. The utility of RBM$^{GABA}$ -assisted STL method was demonstrated by the synthesis of rabbit S-palm sarcolipin (SLN) and the S-palm matrix-2 (M2) ion channel. The synthesis of S-palm membrane proteins highlights the importance of developing non-NCL methods for chemical protein synthesis.
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