934476-97-8Relevant academic research and scientific papers
Enantioselective Enzymatic Reduction of Acrylic Acids
An, Chihui,Shaw, Megan H.,Tharp, Annika,Verma, Deeptak,Li, Hongming,Wang, Heather,Wang, Xiao
supporting information, p. 8320 - 8325 (2020/11/03)
An ene-reductase (ERED 36) with broad substrate specificity was identified, and optimization studies led to the development of an enzymatic protocol for the reduction of α,β-unsaturated acids under mild, aqueous conditions. The substrate scope includes aromatic- A nd aliphatic-substituted acrylic acids, as well as cyclic α,β-substituted acrylic acids, yielding chiral α-substituted acids with exquisite levels of enantioselectivity (>99% ee).
Enantioselective [3 + 2] cycloaddition of allenes to acrylates catalyzed by dipeptide-derived phosphines: Facile creation of functionalized cyclopentenes containing quaternary stereogenic centers
Han, Xiaoyu,Wang, Youqing,Zhong, Fangrui,Lu, Yixin
supporting information; experimental part, p. 1726 - 1729 (2011/04/17)
A new family of dipeptide-based chiral phosphines was designed and prepared. d-Thr-l-tert-Leu-derived catalyst 4c promoted [3 + 2] cycloaddition of allenoates to α-substituted acrylates in a regiospecific and stereoselective manner, furnishing functionalized cyclopentenes with quaternary stereogenic centers in high yields and with excellent enantioselectivities.
3-Mercaptopropionic acids as efficacious inhibitors of activated thrombin activatable fibrinolysis inhibitor (TAFIa)
Islam, Imadul,Bryant, Judi,May, Karen,Mohan, Raju,Yuan, Shendong,Kent, Lorraine,Morser, John,Zhao, Lei,Vergona, Ron,White, Kathy,Adler, Marc,Whitlow, Marc,Buckman, Brad O.
, p. 1349 - 1354 (2007/10/03)
A novel series of cyclic potent, selective, small molecule, thiol-based inhibitors of activated thrombin activatable fibrinolysis inhibitor (TAFIa) and the crystal structures of TAFIa inhibitors bound to porcine pancreatic carboxypeptidase B are described. Three series of cyclic arginine and lysine mimetic inhibitors vary significantly in their selectivity against other human basic carboxypeptidases, carboxypeptidase N and carboxypeptidase B. (-)2a displays TAFIa IC50 = 3 nM and 600-fold selectivity against CPN. Inhibition of TAFIa with (rac)2a resulted in dose dependent acceleration of human plasma clot lysis in vitro and was efficacious as an adjunct to tPA in an in vivo rabbit jugular vein thrombolysis model.
