QUANTIFICATION OF PREGABALIN AND ETORICOXIB COMBO IN TABLETS AND BULK WITH DEVELOPED RP-HPLC METHOD: STABILITY INDICATING FEATURE ASSESSMENT

This investigation reports a stability indicating HPLC method to quantify Pregabalin (PGBN) and etoricoxib (ERCB) in tablets form and bulk form. The PGBN and ERCB were quantified on Thermo C18 column with Orthophosphoric acid (0.1%), and methanol 60:40 vol/vol ratio was employed as mobile phase. The amounts of PGBN and ERCB were enumerated by detector fixed at 236 nm. The procedure demonstrated reasonable linearity for PGBN with R2 = 0.9998 in the quantity scale 37.5 to 112.5 µg/ml, and for ERCB with R2 = 0.9999 in the quantity scale 30 to 90 µg/ml. The LOD as well as LOQ for PGBN are 0.201µg/ml 6 0.670 µg/ml and for ERCB are 0.106 µg/ml 6 0.355 µg/ml. The RT’s for PGBN was 2.636 min and ERCB was 5.607 min and whole analysis time was 8 min. Stability degradation experiments were used to establish the method's capacity to indicate stability indicating. The conditions include acid forced hydrolysis, thermal forced degradation, alkali forced hydrolysis, oxidative forced degradation and photo forced degradation conditions. Detection as well as quantification of PGBN and ERCB was unaffected by the degradants.</jats:p

Enzymatic approach to the synthesis of chiral intermediate of Rodatristat ethyl

Ketoreductases are widely explored for the reduction of prochiral ketones for the preparation of chiral alcohols. Though, the chiral Ir(III) catalyst has been used for the asymmetric reduction of keto intermediate of Rodatristat ethyl, an enzymatic approach for its preparation has not yet been reported. In this regard, we report, for the first time the preparation of enantiopure secondary alcohols (R-3) and (S-3) from 1-(5-chloro-[1,1’-biphenyl]-2-yl)-2,2,2-trifluoroenthan-1-one (2) using commercially available ketoreductases at 30 °C in the presence of 125 mM sodium phosphate buffer pH 6 over 24 h. This enzymatic approach provides the (R)-3 and (S)-3 chiral alcohols in >99% enantiomeric excess (ee) with >99% conversion using KRED-244 and KRED-101 respectively. Furthermore, the KRED-244 and KRED-101 enzymes have been successfully immobilized with sodium alginate, which makes them recyclable and reusable in subsequent reactions. The reusability experiments were carried out over 15 cycles without any apparent loss of activity even after 10 cycles. It is a sustainable approach to the synthesis of enantiopure intermediates of rodatristat ethyl, contributing to the advancement of green chemistry.</p