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Analysis of the interaction between alpha-1-acid glycoprotein and tamoxifen and its metabolites.

Tamoxifen is administered for the treatment of breast cancer; however resistance to therapy is commonplace. Postulated mechanisms of resistance to tamoxifen include altered pharmacology of the drug, changes in the structure and function of the oestrogen receptor and expression of genes that function to support the growth of cells resistant to tamoxifen. However, binding of drugs to proteins found in the plasma is known to affect the efficacy of drugs and alter their distribution. It is already known that tamoxifen is bound 99% to albumin. We investigated the interaction between the plasma protein, alpha-1-acid glycoprotein (AGP), and tamoxifen, since if binding did occur then the free plasma concentration of the drug would be reduced, resulting in the minimum effective concentration of tamoxifen not being attained. Using a recently described intrinsic fluorescence technique for the study of drug-protein interactions, the extent of binding between tamoxifen citrate and AGP was determined. Furthermore, analysis of binding of the known active metabolites of tamoxifen (4-hydroxytamoxifen, N-desmethyltamoxifen, N-desdimethyltamoxifen, cis-alpha-hydroxytamoxifen and trans-alpha-hydroxytamoxifen) to AGP was conducted. Tamoxifen citrate and metabolites were shown to bind AGP, however the level of interaction was low and negligible at the concentration of the drug found in the plasma.