826-18-6Relevant articles and documents
COMPARAISON ENTRE LE ROLE DE L'EAU ET CELUI D'UN ETHER COURONNE DANS LE CADRE DE LA REACTION DE WITTIG REALISEE EN MILIEU HETEROGENE : LIQUIDE-SOLIDE
Delmas, M.,Bigot, Y. Le,Gaset, A.
, p. 4831 - 4834 (1980)
The similar results issued from the use of water and the 18-crown-6 ether for the Wittig reaction (in liquid-solid two-phase system) allowed us to obtain vary high yields in olefin starting from aromatic as well as aliphatic aldehydes.
Stereoselective Rhodium-Catalyzed Isomerization of Stereoisomeric Mixtures of Arylalkenes
Yang, Hongxuan,Dong, Wenke,Wang, Wencan,Li, Tao,Zhao, Wanxiang
supporting information, p. 2833 - 2840 (2020/10/06)
A new efficient method for the synthesis of a high ratio of E -alkenes from E / Z mixtures of alkenes with B 2pin 2in the presence of a rhodium catalyst is described. This reaction features mild reaction conditions, broad functional group tolerance, and highly great application potential.
Highly Selective and Potent Human β-Secretase 2 (BACE2) Inhibitors against Type 2 Diabetes: Design, Synthesis, X-ray Structure and Structure–Activity Relationship Studies
Ghosh, Arun K.,Brindisi, Margherita,Yen, Yu-Chen,Lendy, Emma K.,Kovela, Satish,Cárdenas, Emilio Leal,Reddy, Bhavanam Sekhara,Rao, Kalapala Venketeswara,Downs, Deborah,Huang, Xiangping,Tang, Jordan,Mesecar, Andrew D.
, p. 545 - 560 (2019/02/13)
Herein we present the design, synthesis, and biological evaluation of potent and highly selective β-secretase 2 (memapsin 1, beta-site amyloid precursor protein cleaving enzyme 2, or BACE 2) inhibitors. BACE2 has been recognized as an exciting new target for type 2 diabetes. The X-ray structure of BACE1 bound to inhibitor 2 a {N3-[(1S,2R)-1-benzyl-2-hydroxy-3-[[(1S,2S)-2-hydroxy-1-(isobutylcarbamoyl)propyl]amino]propyl]-5-[methyl(methylsulfonyl)amino]-N1-[(1R)-1-phenylpropyl]benzene-1,3-dicarboxamide} containing a hydroxyethylamine isostere was determined. Based on this structure, a computational docking study was performed which led to inhibitor 2 a-bound BACE2 models. These were used to optimize the potency and selectivity of inhibitors. A systematic structure–activity relationship study led to the identification of determinants of the inhibitors’ potency and selectivity toward the BACE2 enzyme. Inhibitors 2 d [N3-[(1S,2R)-1-benzyl-2-hydroxy-3-[[(1S,2S)-2-hydroxy-1-(isobutylcarbamoyl)pentyl]amino]propyl]-N1-methyl-N1-[(1R)-1-phenylpropyl]benzene-1,3-dicarboxamide; Ki=0.031 nm, selectivity over BACE1: ≈174 000-fold] and 3 l [N1-((2S,3R)-3-hydroxy-1-phenyl-4-((3-(trifluoromethyl)benzyl)amino)butan-2-yl)-N3,5-dimethyl-N3-((R)-1-phenylethyl)isophthalamide; Ki=1.6 nm, selectivity over BACE1: >500-fold] displayed outstanding potency and selectivity. Inhibitor 3 l is nonpeptide in nature and may pave the way to the development of a new class of potent and selective BACE2 inhibitors with clinical potential.
