1123173-71-6

Basic information

• Product Name: C₂₇H₃₇FN₂O₄S
• CAS NO: 1123173-71-6
• Molecular Weight: 504.666
• Mol File: 1123173-71-6.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₂₇H₃₇FN₂O₄S(CAS DataBase Reference)
• NIST Chemistry Reference: C₂₇H₃₇FN₂O₄S(1123173-71-6)
• EPA Substance Registry System: C₂₇H₃₇FN₂O₄S(1123173-71-6)

Safety Data

• Hazardous Substances Data: 1123173-71-6(Hazardous Substances Data)

Upstream product

• 1123173-00-1 (3R,4S,5S)-3-((3-(tert-butyl)benzyl)-amino)-5-(3,5-difluoro-4-nitrobenzyl)-4-hydroxytetrahydro-2H-thiothiopyran 
• 1204343-82-7 (3R,4S,5S)-3-amino-5-(3,5-difluoro-4-nitrobenzyl)-4-hydroxytetrahydro-2H-thiopyran 1,1-dioxide hydrochloride 
• 67567-26-4 4-bromo-2,6-difluoroaniline 
• 147808-42-2 5-bromo-1,3-difluoro-2-nitro-benzene 
• 1123172-99-5 ((3R,4S,5S)-5-(3,5-difluoro-4-nitrobenzyl)-4-hydroxy-1,1-dioxidotetrahydro-2H-thiopyran-3-yl)carbamate 
• 1123172-90-6 5-(bromomethyl)-1,3-difluoro-2-nitro-benzene 
• 1123172-89-3 (3,5-difluoro-4-nitrophenyl)methanol 
• 1123172-87-1 methyl 3,5-difluoro-4-nitrobenzoate 
• 1123172-88-2 3,5-difluoro-4-nitro-benzonitrile 

Relevant articles and documents

Discovery of cyclic sulfone hydroxyethylamines as potent and selective β-site APP-cleaving enzyme 1 (BACE1) inhibitors: Structure-based design and in vivo reduction of amyloid β-peptides

Structure-based design of a series of cyclic hydroxyethylamine BACE1 inhibitors allowed the rational incorporation of prime- and nonprime-side fragments to a central core template without any amide functionality. The core scaffold selection and the structure-activity relationship development were supported by molecular modeling studies and by X-ray analysis of BACE1 complexes with various ligands to expedite the optimization of the series. The direct extension from P1-aryl- and heteroaryl moieties into the S3 binding pocket allowed the enhancement of potency and selectivity over cathepsin D. Restraining the design and synthesis of compounds to a physicochemical property space consistent with central nervous system drugs led to inhibitors with improved blood-brain barrier permeability. Guided by structure-based optimization, we were able to obtain highly potent compounds such as 60p with enzymatic and cellular IC50 values of 2 and 50 nM, respectively, and with >200-fold selectivity over cathepsin D. Pharmacodynamic studies in APP51/16 transgenic mice at oral doses of 180 μmol/kg demonstrated significant reduction of brain Aβ levels.