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21.11.7 Chemoselective Ligation Methods Based on the Concept of Native Chemical Ligation

DOI: 10.1055/sos-SD-121-00066

Malins, L. R.; Payne, R. J.Science of Synthesis Knowledge Updates, (20213193.

General Introduction

Strategies for the chemical synthesis of proteins have led to transformational advances in our understanding of protein structure and our ability to design and exploit protein function for applications in biology and medicine. However, given the size limitations of solid-phase peptide synthesis (SPPS), the construction of larger peptides and proteins through chemical synthesis inherently relies on strategies that selectively link discrete peptide fragments. To this end, chemoselective ligation strategies, which forge interpeptide amide bonds in aqueous solution by harnessing the mutual reactivity of functionalized peptide precursors, have contributed enormously to the field of peptide and protein science. The rapid and sustained adoption of such techniques is due, in large part, to their operational simplicity and ability to exploit unprotected peptide substrates.

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