Metal Ions Enhance the Affinities of Flavonoids for Human Serum Albumin in Vitro

被引:6
|
作者
Yang, Fan [1 ]
Wang, Jie [1 ]
Liu, Chunxi [1 ]
Xu, Xiaochen [1 ]
Shan, Shunan [1 ]
Xia, Zhihua [1 ]
Sun, Xiaowei [1 ]
机构
[1] Shanghai Normal Univ, Coll Life & Environm Sci, Dept Biol, Shanghai 200234, Peoples R China
基金
上海市自然科学基金;
关键词
Flavonoids; Human serum albumin; Metal ions; Affinity; BINDING; INHIBITION; NI2+; RING; BSA; HSA;
D O I
10.1007/s10953-012-9846-z
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The affinities of apigenin, chrysin, daidzein and quercetin for human serum albumin (HSA) were studied in the presence and absence of Pb2+, Ni2+, Zn2+, Mg2+ and Mn2+. The fluorescence intensities of HSA decrease remarkably with increasing concentration of these four flavonoids. Adding apigenin and chrysin resulted in blue-shifts of HSA from lambda (em)=336 to 332 nm and 330 nm, respectively. However, quercetin showed an obvious red-shift of HSA from lambda (em)=336 to 347 nm whereas daidzein hardly affected the lambda (em) of HSA. The lambda (em) shifts induced by flavonoids in the presence of mental ions were much bigger than those in the absence of these ions. Pb2+, Ni2+, Zn2+, Mg2+ and Mn2+ increased the quenching constants of these four flavonoids for HSA by 19.2 % to 43 %, 47.7 % to 117 %, 23.3 % to 64.4 %, 9.29 % to 42.2 % and 18 % to 55.6 %, respectively. The affinities of apigenin, chrysin, daidzein and quercetin for HSA increased about 9.49 %, 3.63 %, 5.73 % and 2.32 %, respectively, in the presence of Pb2+. Ni2+ improved the affinities of apigenin, chrysin, daidzein and quercetin for HSA by about 4.79 %, 0.85 %, 11.91 % and 10.55 %, respectively. Zn2+ enhanced the affinities of apigenin, chrysin, daidzein and quercetin for HSA by about 1.03 %, 1.34 %, 1.96 % and 13.14 %, respectively. Mg2+ increased the affinities of apigenin, chrysin, daidzein and quercetin for HSA by about 2.03 %, 0.7 %, 1.39 % and 2.07 %, respectively. Mn2+ increased the affinities of apigenin, chrysin, daidzein and quercetin for HSA by about 2.46 %, 6.71 %, 12.3 % and 4.10 %, respectively.
引用
收藏
页码:976 / 993
页数:18
相关论文
共 50 条
  • [31] Luminescence quenching by heavy metal ions of probes based on anthracene, pyrene, and eosin in human serum albumin
    E. V. Naumova
    A. G. Melnikov
    G. V. Melnikov
    Journal of Applied Spectroscopy, 2013, 80 : 159 - 163
  • [32] Investigations of the molecular mechanism of diltiazem binding to human serum albumin in the presence of metal ions, glucose and urea
    Farsad, Sara Asadi
    Haghaei, Hossein
    Shaban, Mina
    Zakariazadeh, Mostafa
    Soltani, Somaieh
    JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2022, 40 (15): : 6868 - 6879
  • [33] ELUCIDATING THE INFLUENCE OF SOME METAL IONS ON THE BINDING OF ANTIMALARIAL DRUGS TO HUMAN SERUM ALBUMIN: SPECTROSCOPIC APPROACH
    Musa, Kabiru Abubakar
    Francis, Jaslene Anne
    Mohamad, Saharuddin B.
    Tayyab, Saad
    REVUE ROUMAINE DE CHIMIE, 2023, 68 (10-12) : 541 - 545
  • [34] Luminescence quenching by heavy metal ions of probes based on anthracene, pyrene, and eosin in human serum albumin
    Naumova, E. V.
    Melnikov, A. G.
    Melnikov, G. V.
    JOURNAL OF APPLIED SPECTROSCOPY, 2013, 80 (02) : 159 - 163
  • [35] Conjugation of a Dipicolyl Chelate to Polypeptide Conjugates Increases Binding Affinities for Human Serum Albumin and Survival Times in Human Serum
    Balliu, Aleksandra
    Baltzer, Lars
    CHEMBIOCHEM, 2017, 18 (14) : 1408 - 1414
  • [36] Investigation on the differences of four flavonoids with similar structure binding to human serum albumin
    Chao-Zhan Lin
    Min Hu
    Ai-Zhi Wu
    Chen-Chen Zhu
    Journal of Pharmaceutical Analysis, 2014, 4 (06) : 392 - 398
  • [37] BINDING LEVELS OF URATE IONS IN HUMAN SERUM ALBUMIN AND PLASMA
    FARRELL, PC
    POPOVICH, RP
    BABB, AL
    BIOCHIMICA ET BIOPHYSICA ACTA, 1971, 243 (01) : 49 - +
  • [38] INTERACTION OF MN(II) IONS WITH HUMAN SERUM-ALBUMIN
    CHIKVAIDZE, EN
    GENERAL PHYSIOLOGY AND BIOPHYSICS, 1990, 9 (04) : 411 - 414
  • [39] Interaction of Nitroglycerin with Bovine Serum Albumin and the Influence of Metal Ions on the Binding
    Bao, Chengman
    Wang, Jialian
    Tong, Xuehong
    Zhang, Chunli
    Tang, Xinhui
    JOURNAL OF THE CHEMICAL SOCIETY OF PAKISTAN, 2020, 42 (02): : 180 - 187
  • [40] Effecting of Metal Ions on the Interaction between Zidovudine and Bovine Serum Albumin
    Shao Shuang
    Qiu Jin
    ACTA PHYSICO-CHIMICA SINICA, 2009, 25 (07) : 1342 - 1346