167026-40-6

Upstream product

• 124379-29-9 (4S)-4-(3,4-dichlorophenyl)-1-tetralone 
• 195388-55-7 (+)-(1R)-4-(3,4-dichlorophenyl)-1,2-dihydronaphthalen-1-ol 
• 79560-19-3 4-(3,4-dichlorophenyl)-3,4-dihydro-2H-naphthalen-1-one 
• 195388-54-6 (R)-4-tert-butyl(4-(3,4-dichlorophenyl)-1,2-dihydronaphthalen-1-yloxy)diphenylsilane 
• 1026451-65-9 tert-Butyl-((R)-3,4-dibromo-1,2,3,4-tetrahydro-naphthalen-1-yloxy)-diphenyl-silane 
• 195388-53-5 (R)-4-bromo-1-tert-butyldiphenylsiloxy-1,2-dihydro-naphthalene 
• 195388-52-4 (R)-1-tert-butyldiphenylsiloxy-1,2-dihydro-naphthalene 
• 123849-23-0 (R)-(+)-1-hydroxy-1,2-dihydronaphthalene 
• 439134-46-0 1-(3,4-dichlorophenyl)-1,2-dihydronaphthalene 
• 95-50-1 1,2-dichloro-benzene 
• 90-15-3 α-naphthol 

Downstream Products

• 87857-41-8 norsertraline 
• 79617-96-2 Sertraline 
• 79951-46-5 trans-(1R,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthalenamine 
• 312620-93-2 (S)-N-(4-(3,4-dichlorophenyl)-3,4-dihydronaphthalen-1(2H)-ylidene)methanamine 
• 195388-56-8 (1S,4S)-1-azido-4-(3,4-dichloro-phenyl)-1,2,3,4-tetrahydro-naphthalene 
• 124379-29-9 (4S)-4-(3,4-dichlorophenyl)-1-tetralone 

Relevant academic research and scientific papers

Chemoenzymatic Synthesis of Sertraline

A chemoenzymatic approach has been developed for the preparation of sertraline, an established anti-depressant drug. Ketoreductases (KREDs) were employed to yield a key chiral precursor. The bioreduction of the racemic tetralone exhibited excellent enantioselectivity (>99 % ee) and diastereomeric ratio (99:1) at 29 % conversion (the maximum theoretical yield is 50 %) after 7 hours. The resulting (S,S)-alcohol was efficiently oxidized to an enantiopure (S)-ketone, an immediate precursor of sertraline, by using sodium hypochlorite as oxidant and 2-azaadamantane N-oxyl (AZADO) as organocatalyst. Alternative routes aiming at the direct biocatalytic amination using imine reductases and transaminases were unsuccessful.

Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst

Evaluation of an esterase annotated as 26D isolated from a marine metagenomic library is described. Esterase 26D was found to have a unique substrate scope, including synthetic transformations which could not be readily effected in a synthetically useful manner using commercially available enzymes. Esterase 26D was more selective towards substrates which had larger, more sterically demanding substituents (i. e. iso-propyl or tert-butyl groups) on the β-carbon, which is in contrast to previously tested commercially available enzymes which displayed a preference for substrates with sterically less demanding substituents (e.g. methyl group) at the β-carbon. (Figure presented.).

Efficient kinetic resolution in hydroboration of 1,2-dihydronaphthalenes

1-Substituted 1,2-dihydronaphthalenes undergo kinetic resolution during asymmetric hydroboration with Rh-QUINAP complexes.

Selective functionalization of 1,2-dihydronaphthalenols leads to a concise, stereoselective synthesis of sertraline

Asymmetric reductive ring opening of oxabenzonorbornadiene provides dihydronaphthalenols in high ee and good yield. Functionality present in this system can be used to elaborate the core towards a number of targets. As an illustration, a concise stereoselective synthesis of the important antidepressant sertraline is described.