1227161-30-9

Upstream product

• 375-72-4 Nonafluorobutanesulfonyl fluoride 
• 83110-00-3 diethyl 5-chloro-2-hydroxyphenyl phosphonate 

Downstream Products

• 639517-01-4 (5-chloro-2-cyclopropylethynyl-phenyl)-phosphonic acid diethyl ester 
• 639516-97-5 [5-chloro-2-(4-nitro-phenylethynyl)-phenyl]phosphonic acid diethyl ester 
• 639516-96-4 [5-chloro-2-(4-ethyl-phenylethynyl)-phenyl]-phosphonic acid diethyl ester 
• 639516-95-3 (5-chloro-2-phenylethynyl-phenyl)-phosphonic acid diethyl ester 
• 639516-94-2 (5-chloro-2-hex-1-ynyl-phenyl)-phosphonic acid diethyl ester 
• 1227161-31-0 5-chloro-2-(2-(4-methoxyphenyl)ethynyl)phenylphosphonic acid diethyl ester 
• 1335044-35-3 [5-chloro-2-((E)-styryl)phenyl]phosphonic acid diethyl ester 
• 1335044-52-4 [5-chloro-2-((Z)-2-cyanovinyl)phenyl]phosphonic acid diethyl ester 
• 1335044-34-2 [5-chloro-2-((E)-2-cyanovinyl)phenyl]phosphonic acid diethyl ester 
• 1335044-27-3 (E)-3-[4-chloro-2-(diethoxyphosphoryl)phenyl]acrylic acid methyl ester 
• 1441367-88-9 {5-chloro-2-[(E)-2-(4-fluorophenyl)vinyl]phenyl}phosphonic acid diethyl ester 
• 1441367-94-7 [5-chloro-2-((E)-2-cyclopropylvinyl)phenyl]phosphonic acid diethyl ester 
• 1441368-01-9 {5-chloro-2-[(E)-hex-1-en-1-yl]phenyl}phosphonic acid diethyl ester 

Relevant academic research and scientific papers

Phosphaisocoumarins as a new class of potent inhibitors for pancreatic cholesterol esterase

Due to the importance of pancreatic cholesterol esterase (CEase) as a potential target in atherosclerosis and for the development of hypocholesterolemic agents, there are increasing interests in designing and synthesizing CEase inhibitors. In the present study, we prepared forty-five isocoumarin phosphorus analogues (i.e., phosphaisocoumarins) and investigated the inhibition of these compounds on the CEase. The results showed that some phosphaisocoumarins could act as potent inhibitors of CEase. The most potent inhibitors, compounds 9d, 10a and 12e give IC50 values of 4.8?μM, 2.3?μM and 1.9?μM, respectively. The inhibition mechanism and kinetic characterization studies indicate that they are reversible competitive inhibitors.