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Click Chemistry In Situ: Acetylcholinesterase as a Reaction Vessel for the Selective Assembly of a Femtomolar Inhibitor from an Array of Building Blocks
Author(s) -
Lewis Warren G.,
Green Luke G.,
Grynszpan Flavio,
Radić Zoran,
Carlier Paul R.,
Taylor Palmer,
Finn M. G.,
Sharpless K. Barry
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020315)41:6<1053::aid-anie1053>3.0.co;2-4
Subject(s) - cycloaddition , chemistry , acetylcholinesterase , click chemistry , adduct , enzyme , in situ , stereochemistry , triazole , analyte , combinatorial chemistry , biochemistry , organic chemistry , catalysis , chromatography
Form‐fitting chemistry in a protein mold is enabled by the use of the 1,3‐dipolar cycloaddition of azides and alkynes. The enzyme acetylcholinesterase preferentially assembles one pair of these reactants, each of which bears a group that binds to adjacent positions on the protein structure (see picture), into a 1,2,3‐triazole adduct that is the most potent noncovalent inhibitor of the enzyme yet developed.