676464-29-2

Upstream product

• 32786-26-8 1-phenylethyl 2-methoxyacetate 
• 6604-06-4 (+/-)-trans-2-phenyl-cyclopentylamine 
• 141-78-6 ethyl acetate 
• 2362-73-4 (1R,2R)-(-)-cis-2-Phenylcyclopentanol 
• 100-58-3 phenylmagnesium bromide 
• 285-67-6 Cyclopentene oxide 
• 38805-89-9 (1S,2R)-2-phenylcyclopentanol 

Relevant academic research and scientific papers

ERK INHIBITORS

The present invention provides a compound of Formula (I) or the pharmaceutically acceptable salts, esters, and prodrugs thereof, which are ERK2 inhibitors. The invention also provides a pharmaceutical composition comprising an effective amount of at least one compound of Formula (I) and a pharmaceutically acceptable carrier. The invention also provides a pharmaceutical composition comprising an effective amount of at least one compound of Formula (I) and an effective amount of at least one other pharmaceutically active ingredient (such as, for example, a chemotherapeutic agent), and a pharmaceutically acceptable carrier.

Kinetic resolution of (±)-trans- and (±)-cis-2- phenylcyclopentanamine by CALB-catalyzed aminolysis of esters: The key role of the leaving group

Kinetic resolution of (±)-trans- and (±)-cis-2- phenylcyclopentanamine is effectively performed by lipase B from Candida antarctica, (CALB)-catalyzed aminolysis reaction. Whereas reaction between (±)-trans-2-phenylcyclopentanamine and ethyl acetate proceeds with a very high E value (>200) and conversion (50%), the corresponding acetylation of (±)-cis-2-phenylcyclopentanamine happens with low E value (16) and conversion (28%). Nevertheless, this problem is overcome using other acyl donors such as (±)-1-phenylethyl and (±)-cis-2-phenylcyclopentyl methoxyacetates. The influence of the acyl donor on the CALB-catalyzed aminolysis of (±)-cis-2-phenylcyclopentanamine is also studied.