The title compound 1β-hydroxydigitoxigenin（1） was isolated from the ethanol extract of the roots of Streptocaulon juventas. The crystal structure of 1, C23H34O5·H2O, was determined by Synchrotron X-ray diffrac...The title compound 1β-hydroxydigitoxigenin（1） was isolated from the ethanol extract of the roots of Streptocaulon juventas. The crystal structure of 1, C23H34O5·H2O, was determined by Synchrotron X-ray diffraction analysis due to small crystal size（0.14 mm × 0.04 mm × 0.01 mm）. The crystal belongs to monoclinic, space group P21, with a = 7.6624（15）, b= 13.460（3）, c = 10.370（2） A, b = 92.40（3）°, V = 1068.6（4）A^3, Z = 2, Mr = 406.50, Dx = 1.263 g/cm^3, λ（synchrotron） = 1.2399 A, μ（synchrotron 1.23990） = 0.333 cm^-1, F（000） = 550, S = 1.059, R = 0.0625 and wR = 0.1687 for 4247 unique reflections, of which 3687 were observed（I 〉 2σ（I））. The asymmetric unit contains one independent molecule of 1 and one water molecule which are connected through hydrogen bonds. The conformation of 1 in crystalline state is in good agreement with the solution structure in methanol as indicated by ^1H-NMR analysis. The absolute configuration of 1 could be assigned by referring to the known configuration of the lactone ring at C（17b）. In the solid state, intermolecular hydrogen bonds involving carbonyl group in the lactone moiety and the hydroxyl groups in the steroid moiety ester linked adjacent molecules into a three-dimensional network. Compound 1 showed significant inhibition on Na^＋/K^＋-ATPase with an IC50 of 2.46 mM, which is stronger thiocarbonylbufalin but weaker than a close analog digitoxigenin, suggesting that a lactone ring is important and the substitution of a hydroxyl group at C（1） is not favored for the inhibition of Na^＋/K^＋-ATPase.展开更多
The title compound △14,15-anhydro-24-thiocarbonylbufalin （1） was prepared by the reaction of natural product bufalin with Lawesson reagent. The crystal structure of 1, C24H3002S＇C24H3002S, was determined by single...The title compound △14,15-anhydro-24-thiocarbonylbufalin （1） was prepared by the reaction of natural product bufalin with Lawesson reagent. The crystal structure of 1, C24H3002S＇C24H3002S, was determined by single-crystal X-ray diffraction analysis. It belongs to monoclinic, space group C2, with a = 30.9845（2）, b = 6.8036（3）, c = 22.5791（15）/k, V= 4241.7（4） A3, Mr = 384.21, Z = 4, Dc= 1.204 g/cm3,μ = 1.463 mm4, F（000） = 1664, S = 1.064, R = 0.0487 and wR = 0.0645 for 4683 unique reflections, of which 3757 were observed （I 〉 2σ（/））. The asymmetric unit contains two independent molecules （ⅠandⅡ）, which are closely similar to each other except for the orientation of the lactone ring. Both conformations of I and II are in good agreement with the solution structure in methanol as indicated by 1H-NMR analysis. Due to the presence of heavy atom sulfur in the molecules, the final refinement resulted in a small Flack parameter 0.02（3）, permitting the assignments of the absolute configuration. In the solid state, intermolecular hydrogen bonds involving thiocarbonyl group in the lactone moiety and the hydroxyl groups in the steroid moiety ester linked adjacent molecules into a three-dimensional network. Compound 1 showed weak inhibition on Na＋/K＋-ATPase in contrast to the strong inhibitory activity of the parent compound bufalin, suggesting that the carbonyl group in lactone moiety and the hydroxyl group atC-14 play important roles for the inhibition of Na＋/K＊-ATPase.展开更多
基金supported by the National Natural Science Foundation of China(No.81373956,81274064 and 81573315)the Fundamental Research Funds for the Central Universities(2015ZD010)the Priority Academic Program Development of Jiangsu Higher Education Institutions and Guangzhou Industry-University Collaborative Innovation Major Projects(201508030016)
文摘The title compound 1β-hydroxydigitoxigenin（1） was isolated from the ethanol extract of the roots of Streptocaulon juventas. The crystal structure of 1, C23H34O5·H2O, was determined by Synchrotron X-ray diffraction analysis due to small crystal size（0.14 mm × 0.04 mm × 0.01 mm）. The crystal belongs to monoclinic, space group P21, with a = 7.6624（15）, b= 13.460（3）, c = 10.370（2） A, b = 92.40（3）°, V = 1068.6（4）A^3, Z = 2, Mr = 406.50, Dx = 1.263 g/cm^3, λ（synchrotron） = 1.2399 A, μ（synchrotron 1.23990） = 0.333 cm^-1, F（000） = 550, S = 1.059, R = 0.0625 and wR = 0.1687 for 4247 unique reflections, of which 3687 were observed（I 〉 2σ（I））. The asymmetric unit contains one independent molecule of 1 and one water molecule which are connected through hydrogen bonds. The conformation of 1 in crystalline state is in good agreement with the solution structure in methanol as indicated by ^1H-NMR analysis. The absolute configuration of 1 could be assigned by referring to the known configuration of the lactone ring at C（17b）. In the solid state, intermolecular hydrogen bonds involving carbonyl group in the lactone moiety and the hydroxyl groups in the steroid moiety ester linked adjacent molecules into a three-dimensional network. Compound 1 showed significant inhibition on Na^＋/K^＋-ATPase with an IC50 of 2.46 mM, which is stronger thiocarbonylbufalin but weaker than a close analog digitoxigenin, suggesting that a lactone ring is important and the substitution of a hydroxyl group at C（1） is not favored for the inhibition of Na^＋/K^＋-ATPase.
基金supported by the National Natural Science Foundation of China(81102518)
文摘The title compound △14,15-anhydro-24-thiocarbonylbufalin （1） was prepared by the reaction of natural product bufalin with Lawesson reagent. The crystal structure of 1, C24H3002S＇C24H3002S, was determined by single-crystal X-ray diffraction analysis. It belongs to monoclinic, space group C2, with a = 30.9845（2）, b = 6.8036（3）, c = 22.5791（15）/k, V= 4241.7（4） A3, Mr = 384.21, Z = 4, Dc= 1.204 g/cm3,μ = 1.463 mm4, F（000） = 1664, S = 1.064, R = 0.0487 and wR = 0.0645 for 4683 unique reflections, of which 3757 were observed （I 〉 2σ（/））. The asymmetric unit contains two independent molecules （ⅠandⅡ）, which are closely similar to each other except for the orientation of the lactone ring. Both conformations of I and II are in good agreement with the solution structure in methanol as indicated by 1H-NMR analysis. Due to the presence of heavy atom sulfur in the molecules, the final refinement resulted in a small Flack parameter 0.02（3）, permitting the assignments of the absolute configuration. In the solid state, intermolecular hydrogen bonds involving thiocarbonyl group in the lactone moiety and the hydroxyl groups in the steroid moiety ester linked adjacent molecules into a three-dimensional network. Compound 1 showed weak inhibition on Na＋/K＋-ATPase in contrast to the strong inhibitory activity of the parent compound bufalin, suggesting that the carbonyl group in lactone moiety and the hydroxyl group atC-14 play important roles for the inhibition of Na＋/K＊-ATPase.
