NH<sub>4</sub>I-promoted oxidative formation of benzothiazoles and thiazoles from arylacetic acids and phenylalanines with elemental sulfur
作者:Yujia Xia、Huawen Huang、Wei Hu、Guo-Jun Deng
DOI:10.1039/d1ob00671a
日期:——
NH4I/K3PO4-based catalytic system has been established to enable oxidative formation of thiazole compounds from arylacetic acids and phenylalanines with elemental sulfur. While the three-component reaction of anilines or β-naphthylamines with arylacetic acids and elemental sulfur affords benzo[2,1-d]thiazoles and naphtho[2,1-d]thiazoles, the annulation of phenylalanines with elemental sulfur produces 2-benzyl
已经建立了基于NH 4 I/K 3 PO 4的催化体系,以使得能够从芳基乙酸和苯丙氨酸与元素硫氧化形成噻唑化合物。虽然苯胺或 β-萘胺与芳基乙酸和元素硫的三组分反应产生苯并[ 2,1- d ]噻唑和萘并[ 2,1- d ]噻唑,但苯丙氨酸与元素硫的环化产生 2-苄基和 2-苯甲酰基噻唑。这项工作很好地补充了以前来自其他偶联伙伴的苯并噻唑的三组分环化。
Copper‐Catalyzed Aerobic Oxidation of Amines to Benzothiazoles via Cross Coupling of Amines and Arene Thiolation Sequence
作者:Jihyeon Kim、Kyungsoo Oh
DOI:10.1002/adsc.202000598
日期:2020.9.8
A one‐pot three‐component synthesis of benzothiazoles has been developed using the copper‐catalyzed aerobic cross coupling of amines followed by arene thiolation using elemental sulfur. The dual roles of elemental sulfur and CuCl(OH)‐TMEDA in the aerobic amine oxidation and the aniline thiolation enable the facile access to benzothiazole derivativesfrom readily available starting materials. The operational
Compositions and methods for modulating interaction between polypeptides
申请人:Kazantsev G. Aleksey
公开号:US20050239833A1
公开(公告)日:2005-10-27
The present invention is based, in part, on assays we conducted that revealed compounds that may be used to treat or prevent diseases characterized by an abnormal or undesirable association of one protein with another.
COMPOSITIONS AND METHODS FOR MODULATING INTERACTION BETWEEN POLYPEPTIDES
申请人:The General Hospital Corporation
公开号:US20130203733A1
公开(公告)日:2013-08-08
The present invention is based, in part, on assays we conducted that revealed compounds that may be used to treat or prevent diseases characterized by an abnormal or undesirable association of one protein with another.