Activity of a tamoxifen-raloxifene hybrid ligand for estrogen receptors at an AP-1 site

  • Bioorg Med Chem Lett. 2001 Dec 17;11(24):3129-31. doi: 10.1016/s0960-894x(01)00646-1.
R V Weatherman  1 ,  D C Carroll ,  T S Scanlan
Affiliations
  • 1. Departments of Pharmaceutical Chemistry and Cellular and Molecular Pharmacology, University of California--San Francisco, CA 94143-0446, USA.
PMID: 11720858 DOI: 10.1016/s0960-894x(01)00646-1
Abstract

To test the effect of ligand flexibility on the selective transcriptional activities of ERalpha and ERbeta from an AP-1 site, an analogue of raloxifene was made that removed the ketone functionality and made the ligand more planar and conformationally more similar to 4-hydroxytamoxifen. Desketoraloxifene was found to be a much stronger activator at an AP-1 site with ERalpha than with ERbeta, mimicking 4-hydroxytamoxifen more than raloxifene.

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