文章摘要
曹伟伟;吴婷;方雅静;程玉鑫;潘思轶;徐晓云;.藜蒿叶中1,4-双咖啡酰奎宁酸的鉴定及双咖啡酰奎宁酸类化合物体外抑制黄嘌呤氧化酶和抑制尿酸钠诱导IL-1β的构效关系[J].中国食品学报,2020,20(2):1-8
藜蒿叶中1,4-双咖啡酰奎宁酸的鉴定及双咖啡酰奎宁酸类化合物体外抑制黄嘌呤氧化酶和抑制尿酸钠诱导IL-1β的构效关系
Identification of 1,4-Di-caffeoylquinic Acid in Artemisia selengensis Turcz Leaves and Structure-Activity Relationship of Di-caffeoylquinic Acids on Inhibiting Xanthine Oxidase and Inhibiting Monosodium Urate Induced IL-1β in Vitro
  
DOI:
中文关键词: 藜蒿叶  双咖啡酰奎宁酸  黄嘌呤氧化酶  尿酸钠诱导的IL-1β  构效关系
英文关键词: Artemisia selengensis Turcz  di-caffeoylquinic acid  xanthine oxidase  monosodium urateinducedIL-1β  structure-activity relationship
基金项目:国家自然科学基金项目(31671894)
作者单位
曹伟伟;吴婷;方雅静;程玉鑫;潘思轶;徐晓云; 华中农业大学食品科学技术学院
 
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中文摘要:
      本文主要鉴定藜蒿叶提取物中双咖啡酰奎宁酸(di-CQA)的结构,并研究其对体外抑制黄嘌呤氧化酶(XOD)和抑制尿酸钠(MSU)诱导的IL-1β的定性构效关系。采用HPLC-Q/TOF-MS鉴定藜蒿叶提取物中diCQA的结构,同时系统研究不同咖啡酸取代位置对di-CQA抑制XOD活性和MSU诱导的IL-1β的影响。结果表明:藜蒿叶提取物中富含5种di-CQA (1,4-diCQA、3,4-diCQA、1,5-diCQA、3,5-diCQA和4,5-diCQA),其中,1,4-diCQA存在于藜蒿叶为首次报道。不同咖啡酸取代位置对di-CQA抑制XOD的影响强弱为:C1取代>C4取代>C5取代>C3取代;不同咖啡酸取代位置对di-CQA抑制MSU诱导的IL-1β的影响强弱为:C1取代>C5取代>C3取代,C4取代≥C5取代。此外,di-CQA抑制XOD的活性与抑制MSU诱导的IL-1β活性具有正相关性,提示di-CQA可能通过抑制XOD发挥抑制MSU诱导的IL-1β的活性。该研究揭示了di-CQA预防高尿酸血症和痛风活性的结构特征,也为进一步利用藜蒿及其它膳食来源的di-CQA作为预防高尿酸血症和痛风的食品提供借鉴。
英文摘要:
      Identification of di-caffeoylquinic acids (di-CQAs) from Artemisia selengensis Turcz leaves and structure-activity relationship of di-CQAs on inhibiting xanthine oxidase (XOD) and inhibiting monosodium urate (MSU) induced IL-1β in vitro were studied. Di-CQAs from Artemisia selengensis Turcz leaves were identified by HPLC-Q/TOF-MS, and the effects of different di-CQAs on inhibiting XOD and inhibiting monosodium urate induced IL-1β were systematically studied. Results showed that five di-CQAs (1,4-diCQA, 3,4-diCQA, 1,5-diCQA, 3,5-diCQA and 4,5-diCQA) were identified in Artemisia selengensis Turcz leaves, and 1,4-diCQA was identified in Artemisia selengensis Turcz leaves in this study for the first time. The XOD inhibitory activity of caffeic acid substitution sites on di-CQAs was ranked as follows: C1 substitution > C4 substitution > C5 substitution > C3 substitution; The MSU-inducedIL-1β inhibitory activity of caffeic acid substitution sites on di-CQAs was ranked as follows: C1 substitution > C5 substitution > C3 substitution, C4 substitution≥ C5 substitution. In addition, the XOD inhibitory activity of di-CQAs was positively correlated with the MSU-induced IL-1β inhibitory activity of them, suggesting that di-CQAs couldinhibit MSU-induced IL-1β via inhibiting XOD. This study provides theoretical basis for studying the biological activities of di-CQAs with different structures, and also gives a reference for the development of di-CQAs from Artemisia selengensis Turcz and other dietary food for the prevention of hyperuricemia and gout.
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