956403-69-3Relevant academic research and scientific papers
Towards Sustainable Amino Acid Derived Organocatalysts for Asymmetric syn-Aldol Reactions
Gerasimchuk, Vasiliy V.,Kucherenko, Alexandr S.,Fakhrutdinov, Artem N.,Medvedev, Michael G.,Nelyubina, Yulia V.,Zlotin, Sergei G.
supporting information, p. 2540 - 2544 (2017/05/12)
The undesirable side-processes responsible for the fast deactivation of primary amino acid derived organocatalysts in asymmetric aldol reactions are identified. A new ionic-liquid-supported (S)-valine-/(S)-α,α-diphenylserinol-derived catalyst (9) is desig
Simple and inexpensive threonine-based organocatalysts for the highly diastereo- and enantioselective direct large-scale syn-aldol and anti-Mannich reactions of α-hydroxyacetone
Wu, Chuanlong,Fu, Xiangkai,Li, Shi
experimental part, p. 1063 - 1073 (2011/10/02)
Simple and inexpensive threonine-based organocatalysts that promote syn-aldol reactions and three-component asymmetric anti-Mannich reactions of α-hydroxyacetone achieving a respectable level of enantioselectivities are reported. The syn-aldol products co
Highly efficient organocatalyzed direct asymmetric aldol reactions of hydroxyacetone and aldehydes
Wu, Xiaoyu,Ma, Zhixiong,Ye, Zhengqing,Qian, Shan,Zhao, Gang
supporting information; experimental part, p. 158 - 162 (2009/09/07)
Novel organocatalysts derived from L-threonine and L-leucine have been synthesized for catalyzing direct aldol reactions of hydroxycetone and unactivated aliphatic aldehydes with as low as 2 mol% loading of the catalyst, good to excellent yields and excel
Highly enantioselective direct syn- and anti-aldol reactions of dihydroxyacetones catalyzed by chiral primary amine catalysts
Luo, Sanzhong,Xu, Hui,Zhang, Long,Li, Jiuyuan,Cheng, Jin-Pei
, p. 653 - 656 (2008/09/19)
We present herein simple primary-tertiary diamine-Bronsted acid conjugates that catalyze both syn- and anti-aldol reactions of dihydroxyacetones (DHAs) with high diastereoselectivities and enantioselectivities. This type of organocatalysts functionally mimics all four DHA aldolases, namely L-fuculose-1-phosphate aldolase, D-tagatose-1,6-diphosphate aldolase, D-fructose-1,6-diphosphate aldolase, and L-rhamnulose-1-phosphate aldolase.
