• EI
  • Scopus
  • 食品科学与工程领域高质量科技期刊分级目录第一方阵T1
  • DOAJ
  • EBSCO
  • 北大核心期刊
  • 中国核心学术期刊RCCSE
  • JST China
  • FSTA
  • 中国精品科技期刊
  • 中国农业核心期刊
  • CA
  • WJCI
  • 中国科技核心期刊CSTPCD
  • 中国生物医学SinoMed
中国精品科技期刊2020
王晶晶, 徐为民, 王道营. 姜黄素与猪脂肪氧合酶相互作用及对蛋白质结构的影响[J]. 食品工业科技, 2020, 41(4): 19-24. DOI: 10.13386/j.issn1002-0306.2020.04.004
引用本文: 王晶晶, 徐为民, 王道营. 姜黄素与猪脂肪氧合酶相互作用及对蛋白质结构的影响[J]. 食品工业科技, 2020, 41(4): 19-24. DOI: 10.13386/j.issn1002-0306.2020.04.004
WANG Jing-jing, XU Wei-min, WANG Dao-ying. Interactions of Curcumin with Porcine Lipoxygenase and Its Effect on Protein Structure[J]. Science and Technology of Food Industry, 2020, 41(4): 19-24. DOI: 10.13386/j.issn1002-0306.2020.04.004
Citation: WANG Jing-jing, XU Wei-min, WANG Dao-ying. Interactions of Curcumin with Porcine Lipoxygenase and Its Effect on Protein Structure[J]. Science and Technology of Food Industry, 2020, 41(4): 19-24. DOI: 10.13386/j.issn1002-0306.2020.04.004

姜黄素与猪脂肪氧合酶相互作用及对蛋白质结构的影响

Interactions of Curcumin with Porcine Lipoxygenase and Its Effect on Protein Structure

  • 摘要: 利用分光光度计法、荧光光谱法以及圆二色谱法(CD)研究姜黄素与猪12-脂肪氧合酶(12-Lipoxygenase,12-LOX)的相互作用。结果表明,姜黄素能够抑制猪12-LOX酶活,并且浓度越高,抑制作用越强,姜黄素抑制12-LOX的IC50值为2.156 μg/mL。荧光光谱结果表明姜黄素对猪12-LOX有较强的荧光猝灭作用,猝灭机制为静态猝灭,两者之间的作用力主要是范德华力和氢键。同步荧光光谱研究表明,姜黄素与猪12-LOX的结合位点更接近于色氨酸残基。圆二色谱结果表明,姜黄素能够与猪12-LOX相互作用,并使LOX二级结构发生变化。

     

    Abstract: The interaction between curcumin and porcine 12-Lipoxygenase(LOX)was investigated by spectrophotometry,fluorescence spectroscopy and circular dichroism(CD). The results showed that curcumin inhibited the activity of porcine 12-LOX.The more concentration it was,the more inhibition effect it behaved. The IC50 value of curcumin inhibited 12-LOX was 2.156 μg/mL. Fluorescence results showed that curcumin had strong quenching effects on porcine 12-LOX,and the quenching mechanism was static quenching. The interaction between curcumin and porcine 12-LOX was mainly van der Waals force and hydrogen bonding. Synchronous fluorescence spectroscopy indicated that the binding site of curcumin to porcine 12-LOX was closer to the tryptophan residue. CD chromatography showed that curcumin interacted with porcine 12-LOX and made the LOX secondary structure changed.

     

/

返回文章
返回