Structure-based design and synthesis of conformationally constrained derivatives of methyl-piperidinopyrazole (MPP) with estrogen receptor (ER) antagonist activity

Document Type

Article

Publication Title

Bioorganic Chemistry

Abstract

Nuclear Estrogen receptors (ER) are cytoplasmic proteins; translocated to the nucleus to induce transcriptional signals after getting bound to the estrogen hormone. ER activation implicated in cancer cell proliferation of female reproductive organs. Thus, the discovery of ER antagonists is a reliable strategy to combat estrogen-dependent breast cancer. Endometrial carcinoma is one of the complications encountered upon long-term therapy by selective estrogen receptor modulators (SERMs) like Tamoxifen (TMX) and methyl piperidinopyrazole (MPP). Thus, the ER-full antagonist is a solution to improve the safety of this class of therapeutics during the treatment of breast cancer. We selected MPP as a lead structure to design conformationally constrained analogs. Structural rigidification is a proven strategy to transform the SERMs into full antagonists. Accordingly, we synthesized 7-methoxy-3-(4-methoxyphenyl)-4,5-dihydro-2H-benzo[g]indazoles (4), (6a-c), (8–12) along with the biphenolic counterparts (13–19) that are the anticipated active metabolites. The 4-nitrophenyl derivative (4) is with the most balanced profile regarding the in vivo anti-uterotrophic potential (EC50 = 4.160 μM); and the cytotoxicity assay of the corresponding active metabolite (13) against ER+ breast cancer cell lines (MCF-7 IC50 = 7.200 μM, T-47D IC50 = 11.710 μM). The inconsiderable uterotrophic activities of the elaborated ER-antagonists and weak antiproliferative activity of the compound (13) against ovarian cancer (SKOV-3 IC50 = 29.800 μM) highlighted it as a good start point to elaborate potential ER-full antagonists devoid of endometrial carcinoma. Extending the pendant chain that protrudes from the 2-(4-(substituted)-phenyl) ring of the new benzo-indazoles is recommended for enhancing the potency based on the binding mode of compound (13) in the ligand-binding domain (LBD) of ER.

DOI

10.1016/j.bioorg.2021.105554

Publication Date

2-1-2022

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