Abstract
Chemoselective ligation reactions provide facile access to various peptides and proteins including cyclic peptides, posttranslationally modified proteins, and peptide/ protein probes. Recently, peptide-ligase-based chemo-enzymatic methods have emerged as promising alternatives to chemical approaches. Ligation mediated by the newly discovered butelase 1 represents one of the state-of-the-art chemo-enzymatic strategies for its high catalytic efficiency and unique substrate specificity. The butelasemediated ligation can be carried out in a semisynthetic manner, in which chemically synthesized peptides and expressed proteins are used as substrates, rendering it suitable for various applications including site-specific modification of proteins and the preparation of thioesters. In this review, we summarize the recent studies and applications of butelase 1.
Keywords: Chemoselective ligation reaction, peptide ligase, butelase 1, peptide/protein drugs, cyclic peptides, protein modification.
Graphical Abstract
Call for Papers in Thematic Issues
Catalytic C-H bond activation as a tool for functionalization of heterocycles
The major topic is the functionalization of heterocycles through catalyzed C-H bond activation. The strategies based on C-H activation not only provide straightforward formation of C-C or C-X bonds but, more importantly, allow for the avoidance of pre-functionalization of one or two of the cross-coupling partners. The beneficial impact of ...read more
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