Inhibition of cholesteryl ester transfer protein by substituted dithiobisnicotinic acid dimethyl ester: involvement Of a critical cysteine.
@article{Hope2000InhibitionOC, title={Inhibition of cholesteryl ester transfer protein by substituted dithiobisnicotinic acid dimethyl ester: involvement Of a critical cysteine.}, author={Hannah Hope and Deborah M. Heuvelman and Kevin L. Duffin and C. Smith and Jeff Zablocki and Roger Schilling and Shraddha Hegde and L M Lee and Bryan J. Witherbee and Mark P. Baganoff and Can Bruce and Alan R. Tall and Elaine S. Krul and Kevin C Glenn and Daniel T. Connolly}, journal={Journal of lipid research}, year={2000}, volume={41 10}, pages={ 1604-14 } }
SC-71952, a substituted analog of dithiobisnicotinic acid dimethyl ester, was identified as a potent inhibitor of cholesteryl ester transfer protein (CETP). When tested in an in vitro assay, the concentration of SC-71952 required for half-maximal inhibition was 1 microm. The potency of SC-71952 was enhanced 200-fold by preincubation of the inhibitor with CETP, and was decreased 50-fold by treatment with dithiothreitol. Analogs of SC-71952 that did not contain a disulfide linkage were less…
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