Peptide or compound synthesis is the crucial step of design for E3 ligase or target protein in PROTAC assay. Peptide synthesis mostly often occurs by coupling the carboxyl group of the incoming amino acid to the N-terminus of the growing peptide chain (C-to-N), which is opposite from protein biosynthesis. Though common methods of peptide synthesis have some critical differences, they all follow the same precise, step-wise and cyclic method to add amino acids one-at-a-time to the growing peptide chain.
Solid phase peptide synthesis (SPPS) is widely recognized technology in chemistry among biologists for its high-speed, versatility, automatization possibility. In SPPS system peptide is anchored to an insoluble, stable support (resin), chemical reactants can freely diffuse into the interior of the resin beads, and the reaction rates are close to those in solution. The peptide is assembled in a stepwise manner by repeated cycles of formation of a peptide bond between the amino group and an Nα-protected amino acid, followed by deprotection of the temporary Nα-protecting group. At the end of the synthesis, the assembled peptide is cleaved from the solid support. Figure 1 shows the SPSS process, where Y is a temporary protective group, the side chains of groups Rn are protected in accordance with their functionality.
Figure 1. General scheme of SPPS.
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1. Marglin A, Merrifield RB. (1970). Chemical Synthesis of Peptides and Proteins. Annual Review of Biochemistry, 39(1), 841–866. doi:10.1146/annurev.bi.39.070170.004205