Addition of Isocyanide-Containing Amino Acids to the Genetic Code for Protein Labeling and Activation.

ABSTRACT: Site-specific introduction of bioorthogonal handles into biomolecules provides powerful tools for studying and manipulating the structures and functions of proteins. Recent advances in bioorthogonal chemistry demonstrate that tetrazine-based bioorthogonal cycloaddition is a particularly useful methodology due to its high reactivity, biological selectivity, and turn-on property for fluorescence imaging. Despite its broad applications in protein labeling and imaging, utilization of tetrazine-based bioorthogonal cycloaddition has been limited to date by the requirement of a hydrophobic strained alkene reactive moiety. Circumventing this structural requirement, we report the site-specific incorporation of noncanonical amino acids (ncAAs) with a small isocyanide (or isonitrile) group into prote

SUBMITTER: Chen Y 

PROVIDER: S-EPMC6925311 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature