Abstract
Chemical modification of proteins with bioorthogonal reaction and site-selectivity has been increasingly recognized for exquisite control over homogeneity and geometry, allowing more complex and various applications of proteins. The development of novel bioorthogonal reactions and their adaptation to protein chemistry in the form of genetically encoded non-natural amino acids are fueling widespread use of the so-called ‘bioorthogonal protein conjugation’. Site-specific incorporation of a non-natural amino acid technique precisely delivers a bioorthogonal group to any defined site in response to an expanded genetic code where a selective bond-forming reaction equips proteins with novel functionalities in a chemically well-defined and homogeneous manner.
Keywords: Non-natural amino acid, bioorthogonal reaction, site-specific incorporation, bioconjugation, protein evolution, genetic code.
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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