The binding mechanisms of plasma protein to active compounds in Alismaorientale rhizomes (Alismatis Rhizoma)

被引:17
作者
Xu, Fei [1 ]
Wu, Qi-nan [1 ]
Chen, Jun [1 ]
Gu, Wei [1 ]
Fang, Fang [1 ]
Zhang, Lin-qun [2 ]
Zhao, Bo [3 ]
机构
[1] Nanjing Univ Chinese Med, Coll Pharm, Nanjing 210023, Jiangsu, Peoples R China
[2] Nanjing Normal Univ, Ctr Anal & Testing, Nanjing 210097, Jiangsu, Peoples R China
[3] Nanjing Normal Univ, Coll Chem & Environm Sci, Nanjing 210097, Jiangsu, Peoples R China
关键词
Active compounds in Alismatis Rhizoma; Ultrafiltration; SDS-PAGE; Fluorescence spectroscopy; Circular dichroism spectroscopy; Molecular modeling; HUMAN SERUM-ALBUMIN; DYNAMICS;
D O I
10.1016/j.bmcl.2014.07.065
中图分类号
R914 [药物化学];
学科分类号
100705 [微生物与生化药学];
摘要
Ultrafiltration and HPLC were employed to assess binding rates between rat plasma protein and two active compounds with lipid-regulating properties (alisol B 23-acetate and alisol A 24-acetate) from Alismaorientale rhizomes (Alismatis Rhizoma), a traditional Chinese medicine. SDS-PAGE was used for the evaluation of the binding between the alisol acetates and Hb in plasma. The fluorescence spectroscopy and circular dichroism spectroscopy were also combined with molecular modeling to explore binding mechanisms between Hb and the alisol acetates under imitative physiological condition. The ultrafiltration results show that alisol B 23-acetate bound more strongly than alisol A 24-acetate to plasma protein. SDS-PAGE results may suggest that alisols bind to Hb in plasma. The spectroscopy results are consisting with the molecular modeling results, and they indicate that the differences in plasma protein binding strength between the two compounds may be related to their side chains. A folded side chain/parent ring bound more strongly to Hb than an open side chain/parent ring. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4099 / 4105
页数:7
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