水溶性阳离子型吡啶基咔咯镓配合物与人血清蛋白的相互作用

doi:10.7503/cjcu20150044

高等学校化学学报 ›› 2015, Vol. 36 ›› Issue (6): 1033.doi: 10.7503/cjcu20150044

• 研究论文: 无机化学 • 上一篇下一篇

水溶性阳离子型吡啶基咔咯镓配合物与人血清蛋白的相互作用

闻金燕¹, 吕标彪², 张阳¹, 王家敏¹, 应晓², 王惠³, 计亮年^3,⁴, 刘海洋^1,³()

1. 华南理工大学化学系
2. 应用物理系, 广州 510641
3. 中山大学光电材料与技术国家重点实验室
4. 生物无机与合成化学教育部重点实验室, 广州 510275

收稿日期:2015-01-14 出版日期:2015-06-10 发布日期:2015-05-22
作者简介:联系人简介: 刘海洋, 男, 博士, 教授, 博士生导师, 主要从事大环化合物和化学生物学研究. E-mail:chhyliu@scut.edu.cn
基金资助:
国家自然科学基金(批准号: 21171057, 21371059, 61178037, 61475196)、广东省自然科学基金(批准号: 10351064101000000, 9351027501000003)和中山大学光电材料与技术国家重点实验室开放基金(批准号: 2014-KF-MS2)资助

Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex^†

WEN Jinyan¹, LÜ Biaobiao², ZHANG Yang¹, WANG Jiamin¹, YING Xiao², WANG Hui³, JI Liangnian^3,⁴, LIU Haiyang^1,^3,^*()

1. Department of Chemistry
2. Department of Applied Physics,South China University of Technology, Guangzhou 510641, China
3. State Key Laboratory of Optoelectronics Materials and Technologies,4. Laboratory of Bioinorganic and Synthetic Chemistry of Ministry of Education,Sun-Yat Sen University, Guangzhou 510275, China
4. Laboratory of Bioinorganic and Synthetic Chemistry of Ministry of Education,Sun-Yat Sen University, Guangzhou 510275, China

Received:2015-01-14 Online:2015-06-10 Published:2015-05-22
Contact: LIU Haiyang E-mail:chhyliu@scut.edu.cn
Supported by:
† Supported by the National Natural Science Foundation of China(Nos.21171057, 21371059, 61178037, 61475196), the Natural Science Foundation of Guangdong Province, China(Nos.10351064101000000, 9351027501000003) and the Open Fund of State Key Laboratory of Opto-electronic Materials and Technology of Sun-Yat Sen University, China(No.2014-KF-MS2)

摘要/Abstract

摘要：

利用紫外吸收光谱、荧光光谱、圆二色(CD)光谱和分子对接计算探究了5,10,15-三[4-(N-甲基-吡啶)]咔咯镓配合物(1-Ga) 与人血清蛋白(HSA) 的相互作用. 结果表明, HSA的荧光能被1-Ga静态猝灭, 两者的结合常数为2.82×10⁴ L/mol, 作用距离为3.342 nm. 热力学参数显示1-Ga主要通过氢键和疏水作用与HSA结合, 位点标记竞争实验表明1-Ga优先结合HSA的布洛芬位点Ⅱ. 此外, 紫外吸收光谱和CD光谱显示二者的相互作用会导致HSA α-螺旋结构的减少. 分子对接计算结果表明1-Ga优先结合在HSA亚结构域ⅢA的位点Ⅱ疏水袋中.

关键词: 咔咯, 镓, 人血清蛋白, 相互作用

Abstract:

The interaction between gallium 5, 10, 15-tris(4-methylpyridiniumyl)corrole(1-Ga) and human serum albumin(HSA) was investigated using UV-Vis spectra, fluorescence spectra, circular dichroism(CD) spectra and molecular docking simulation. The results reveal that the fluorescence quenching of HSA by 1-Ga is a static quenching process. The binding constant of complex 1-Ga with HSA is 2.82×10⁴ L/mol, and bin-ding distance r=3.342 nm. Thermodynamic parameters show the interaction is mainly driven by hydrophobic and hydrogen binding forces. Site marker competition experiment indicates 1-Ga preferably bind to ibuprofen site Ⅱ of HSA. Also, α-helix content of HSA will decrease upon binding 1-Ga as indicated by UV-Vis and CD spectroscopy. Molecular docking simulation confirmed 1-Ga bind to the hydrophobic pocket site Ⅱ in domain ⅢA of HSA.

Key words: Corrole, Gallium, Human serum albumin, Interaction

中图分类号:

O614.37

TrendMD:

闻金燕, 吕标彪, 张阳, 王家敏, 应晓, 王惠, 计亮年, 刘海洋. 水溶性阳离子型吡啶基咔咯镓配合物与人血清蛋白的相互作用. 高等学校化学学报, 2015, 36(6): 1033.

WEN Jinyan, LÜ Biaobiao, ZHANG Yang, WANG Jiamin, YING Xiao, WANG Hui, JI Liangnian, LIU Haiyang. Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex^†. Chem. J. Chinese Universities, 2015, 36(6): 1033.

图/表 13

Fig.1 Structure of gallium 5,10,15-tris(4-methylpyridiniumyl)corrole

Fig.2 Fluorescence spectra of HSA(5 μmol/L) in the absence and presence of 1-Ga in Tris-HCl buffer(A) and the plots of F0/F vs. [1-Ga] before(a) and after(b) IFE correction(B)(A) [1-Ga]/(μmol·L-1) from a to m: 1—12, step 1.

Table 1 Binding parameters of 1-Ga and HSA at pH=7.4

Complex	Stern-Volmer method		Scatchard method
Complex	10^-4K_SV/(L·mol^-1)	10^-12K_q/(L·mol^-1·s^-1)	10^-4K_A/(L·mol^-1)	n
298	2.69	2.69	2.82	0.94
304	2.53	2.53	2.71	0.97
310	2.39	2.39	2.59	1.01

Fig.3 Scatchard plots for HSA and 1-Ga binding at different temperatures

Table 2 Thermodynamic parameters of 1-Ga-HSA interaction at pH=7.4

Complex	ΔH/(kJ·mol^-1)	ΔG/(kJ·mol^-1)	ΔS/(J·mol^-1·K^-1)
298	-5.465	-25.391	66.865
304		-25.792
310		-26.193

Fig.4 Fluorescence spectra changes of HSA-warfarin(A) and HSA-ibuprofen systems(B) with the addition of 1-Ga in Tris-HCl buffer [HSA]=[warfarin]=[ibuprofen]=5 μmol/L, [1-Ga]/(μmol·L-1) from a to l: 1—12, step 1.

Fig.5 Stern-Volmer plots(A) and Scatchard plots(B) for the site marker competitive experiments of 1-Ga-HSA system

Table 3 Binding parameters for site competitive experiments of 1-Ga at pH=7.4, 298 K

Site marker	Stern-Volmer method		Scatchard method
Site marker	10^-4K_SV/(L·mol^-1)	10^-12K_q/(L·mol^-1·s^-1)	10^-4K_A/(L·mol^-1)	n
Blank	2.69	2.69	2.82	0.94
Warfarin	2.03	2.03	2.53	1.09
Ibuprofen	1.35	1.35	1.47	1.05

Fig.6 Overlap of the fluorescence spectra of HSA(a, 1 μmol/L) and the absorption spectra of 1-Ga(b, 1 μmol/L)

Fig.7 UV spectra of HSA(1 μmol/L) in the absence(a) and presence(b) of 1-Ga(10 μmol/L) in Tris-HCl buffer

Fig.8 Synchronous fluorescence spectra of tyrosine(A) and tryptophan(B) in HSA, and F/F0 changes of HSA(5 μmol/L) upon the addition of 1-Ga in Tris-HCl buffer(C)(A) [1-Ga]/(μmol·L-1) from a to k: 0—20, step 2. (B) [1-Ga]/(μmol·L-1) from a to l: 0—22, step 2.

Fig.9 CD spectra changes of HSA(1 μmol/L) in the absence and presence of 1-Ga in Tris-HCl buffer[1-Ga]/(μmol·L-1): a. 0, b. 5 , c. 10, d. 15.

Fig.10 1-Ga docked in the binding pocket of HSA(A) and the amino acid residues around 1-Ga(B)

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水溶性阳离子型吡啶基咔咯镓配合物与人血清蛋白的相互作用

Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex^†

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水溶性阳离子型吡啶基咔咯镓配合物与人血清蛋白的相互作用

Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex†

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Interaction of Human Serum Albumin and Water Soluble Cationic Pyridyl Corrole Gallium Complex^†