Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/12787
Title: Enzymatic synthesis and bioactivity of estradiol derivative conjugates with different amino acids
Authors: Yan, AX
Chan, RYK
Lau, WS
Lee, KS
Wong, MS 
Xing, GW
Tian, GL
Ye, YH
Keywords: Chemoselectivity
Conjugate
Enzymatic synthesis
Estrogen receptor
Steroids
Issue Date: 2005
Publisher: Pergamon Press
Source: Tetrahedron, 2005, v. 61, no. 24, p. 5933-5941 How to cite?
Journal: Tetrahedron 
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.
URI: http://hdl.handle.net/10397/12787
ISSN: 0040-4020
DOI: 10.1016/j.tet.2005.02.090
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