Phosphothreonine as a catalytic residue in peptide-mediated asymmetric transfer hydrogenations of 8-aminoquinolines.
Phosphothreonine as a catalytic residue in peptide-mediated asymmetric transfer hydrogenations of 8-aminoquinolines.
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DOI：
10.1002/anie.201505898
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发表时间：
2015-09-14
期刊：
影响因子：
--
通讯作者：
Miller SJ
中科院分区：
文献类型：
--
作者：
Shugrue CR;Miller SJ
我们报道了磷酸苏氨酸(PThr)插入多肽后，构成了一类新型的手性磷酸(CPA)催化剂。为了证明这些磷酸肽作为不对称催化剂的潜力，我们描述了一种以前未被探索的底物类的对映选择性转移氢化反应，用于CPA催化的还原。含有pThr的多肽与含有C8-氨基的2-取代喹啉对映体选择性高达94：6Er。核磁共振研究表明，氢键相互作用促进了底物与刚性β-Turn催化剂之间的强烈络合。
We report that phosphothreonine (pThr), upon insertion into peptides, constitutes a new class of chiral phosphoric acid (CPA) catalyst. To demonstrate these phosphopeptides’ potential as asymmetric catalysts, we describe enantioselective transfer hydrogenations of a previously unexplored substrate class for CPA-catalyzed reduction. pThr-containing peptides lead to the observation of enantioselectivities of up to 94:6 er 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.