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Phosphothreonine as a Catalytic Residue in Peptide‐Mediated Asymmetric Transfer Hydrogenations of 8‐Aminoquinolines
Author(s) -
Shugrue Christopher R.,
Miller Scott J.
Publication year - 2015
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/anie.201505898
Subject(s) - catalysis , chemistry , residue (chemistry) , phosphoric acid , enantioselective synthesis , hydrogen bond , peptide , organocatalysis , combinatorial chemistry , stereochemistry , substrate (aquarium) , organic chemistry , molecule , biochemistry , oceanography , geology
Phosphothreonine (pThr) was found to constitute a new class of chiral phosphoric acid (CPA) catalyst upon insertion into peptides. To demonstrate the potential of these phosphopeptides as asymmetric catalysts, enantioselective transfer hydrogenations of a previously underexplored substrate class for CPA‐catalyzed reductions were carried out. pThr‐containing peptides lead to the observation of enantioselectivities of up to 94:6 e.r. with 2‐substituted quinolines containing C8‐amino functionality. NMR studies indicate that hydrogen‐bonding interactions promote strong complexation between substrates and a rigid β‐turn catalyst.