Enzymatic synthesis and bioactivity of estradiol derivative conjugates with different amino acids

Ai Xin Yan, Robbie Y.K. Chan, Wai Sum Lau, Kin Sing Lee, Man Sau Wong, Guo Wen Xing, Gui Ling Tian, Yun Hua Ye

Research output: Journal article publicationJournal articleAcademic researchpeer-review

13 Citations (Scopus)

Abstract

A series of N-protected amino acid-estradiol derivative conjugates have been synthesized by coupling of 17β-aminoestra-1,3,5 (10)-trien-3-ol (1) or 17β-hydrazonoestra-1,3,5 (10)-trien-3-ol (2) with different amino acids via the catalysis of subtilisin Carlsberg in organic solvent. Various factors, including the structure of amino acid residue, different N-protecting groups of amino acids, different esters of carboxyl group and water content of the reaction media that influence the efficiency of enzymatic reactions were systematically studied. In vitro biological activity studies revealed that the binding interactions between estradiol derivative conjugates and estrogen receptor can be affected by the properties of the conjugated amino acid, but the effects of the change in binding properties did not result in changes in biological activities in both MCF-7 and HeLa cell lines.
Original languageEnglish
Pages (from-to)5933-5941
Number of pages9
JournalTetrahedron
Volume61
Issue number24
DOIs
Publication statusPublished - 13 Jun 2005

Keywords

  • Chemoselectivity
  • Conjugate
  • Enzymatic synthesis
  • Estrogen receptor
  • Steroids

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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