Formation of Raloxifene Homo-dimer in CYP3A4, Evidence for Multi-substrate Binding in a Single Catalytically Competent P450 Active Site

Davis, J.A., et al., 513(2), 110-118, Arch Biochem Biophys, 2011

Studies were carried out to understand the interactions the polyaromatic compound raloxifene with CYP3A4, and how those interactions relate to raloxifene homo-dimer formation in vitro. Kinetics of raloxifene/CYP3A4 binding were characterized using the Octet RED platform and biotinylated CYP3A4 immobilized on Super Streptavidin biosensors. Data suggested a 2:1 binding relationship between raloxifene and CYP3A4, supporting the conclusion that raloxifene forms a homo-dimer within the CYP3A4 active site.

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