嘧啶衍生物与人血清白蛋白的相互作用

doi:10.7503/cjcu20170063

高等学校化学学报 ›› 2017, Vol. 38 ›› Issue (11): 1982.doi: 10.7503/cjcu20170063

嘧啶衍生物与人血清白蛋白的相互作用

唐乾^1,²(), 苏晋红^2,³, 曹洪玉^1,², 王立皓^2,³, 史飞^2,³, 王爱玲^2,³, 宫婷婷¹, 金晓军^2,³, 郑学仿²()

1. 大连大学生命科学与技术学院, 大连 116622
2. 辽宁省生物有机化学重点实验室, 大连 116622
3. 环境与化学工程学院, 大连 116622

收稿日期:2017-01-26 出版日期:2017-11-10 发布日期:2017-10-30
作者简介:联系人简介: 郑学仿, 男, 博士, 教授, 博士生导师, 主要从事无机生物化学研究. E-mail: dlxfzheng@126.com; 唐乾, 女, 博士, 副教授, 主要从事蛋白质相互作用研究. E-mail: tangqian@dlu.edu.cn
基金资助:
国家自然科学基金(批准号: 21271036, 21571025, 21601023, 21601024, 21601025, 21506018)资助

Interaction of Pyrimidine Derivatives with Human Serum Albumin^†

TANG Qian^1,^2,^*(), SU Jinhong^2,³, CAO Hongyu^1,², WANG Lihao^2,³, SHI Fei^2,³, WANG Ailing^2,³, GONG Tingting¹, JIN Xiaojun^2,³, ZHENG Xuefang^2,^*()

1. College of Life Science and Biotechnology, Dalian 116622, China
2. Liaoning Key Laboratory of Bio-organic Chemistry, Dalian 116622, China
3. School of Environmental and Chemical Engineering, Dalian University, Dalian 116622, China

Received:2017-01-26 Online:2017-11-10 Published:2017-10-30
Contact: TANG Qian,ZHENG Xuefang E-mail:tangqian@dlu.edu.cn;dlxfzheng@126.com
Supported by:
† Supported by the National Natural Science Foundation of China(Nos.: 21271036, 21571025, 21601023, 21601024, 21601025, 21506018)

摘要/Abstract

摘要：

在模拟生理条件下, 运用荧光光谱、激光闪光光解(LFP)和分子对接等技术研究了8种具有抗肿瘤活性的嘧啶衍生物(PDs, 其中PDs A 5-FU为成药, PDs B-H为实验室自制)与人血清白蛋白(HSA)的相互作用. 利用Stern-Volmer方程和激光闪光光解技术分析了PDs对HSA的荧光猝灭机制, PDs A和B为静态猝灭, PDs G和H为动态猝灭. 用双倒数曲线法得出5种PDs与HSA的结合常数K_a和结合位点数n, 在测定条件下5种PDs与载体结合位点数均为1, 且均以弱结合力结合, 通过热力学参数ΔH, ΔS和ΔG推测出PDs B, C和E与HSA之间的作用力为静电作用力和疏水作用力, PDs A和D与HSA之间的作用力是氢键和范德华力, 分子对接结果与其一致. 根据Förster非辐射能量转移理论(FRET)分析了HSA和PDs之间的结合距离(r), 其结果均小于4 nm, 符合能量转移理论. 进一步利用同步荧光、三维荧光和圆二色光谱考察了PDs与HSA结合过程中HSA空间构象的变化, 结果显示, 仅PDs A和C对HSA的芳香族氨基酸周围的疏水性略有增强作用. 体外实验结果表明, HSA可以作为优良的载体来运输和储存PDs A~E, 这为嘧啶衍生物的后续研究提供了可参考的实验数据.

关键词: 人血清白蛋白, 嘧啶衍生物, 三维荧光技术, 激光闪光光解, 分子对接技术

Abstract:

The interaction of eight pyrimidine derivatives(PDs, 5-FU marked as A is the positive control, other seven samples have been made in our laboratory and numbered from B to H, respectively) with human serum albumin(HSA) have been investigated by means of steady state fluorescence, laser flash photolysis(LFP), UV-Vis absorption spectroscopy and molecular docking techniques under simulative physiological coditions. The fluorescence quenching mechanism of HSA and different pyrimidine derivatives have been analyzed by the Stern-Volmer equation and laser flash photolysis techniques. From these results, we can know that pyrimidine derivatives numbered from A to E are static quenching, but pyrimidine derivatives numbered from G to H are dynamic quenching. Depending on double reciprocal curve, we can obtain the binding constants(K_a) and the number of binding sites(n) of the five pyrimidine derivatives of static quenching and HSA. These data show that the protein and pyrimidine derivatives combinate with weak binding force and the number of binding site are equal to one. Fitting the thermodynamic parameters ΔH, ΔS and ΔG can faciliate to understand the binding force types for pyrimidine derivatives and HSA, and pyrimidine derivative B, C and E are the electrostatic and hydrophobic interactions, while for pyrimidine derivatives A and D are hydrogen bond and van der Waals force, and these experimental results are consistent with molecular docking results. According to non-radiative energy transfer theory(FRET), the binding distance(r) between HSA and pyrimidine derivaties can be obtained, which are less than 4 nm, and these results are conform to the energy transfer theory. With synchronous fluorescence, three-dimensional fluorescence and circular dichroism spectroscopy, the space conformation changes of HSA in the drugs combining process can be investigated. The results show that pyrimidine derivatives B, D and E have no influence on the secondary and tertiary structure of HSA. pyrimidine derivative A and C have no effect on secondary structure of HSA, but the hydrophobicity around the aromatic amino acids for the tertiary structure are slightly enhanced. Therefore, HSA can be used as an excellent carrier to transport and store these five pyrimidine derivatives.

Key words: Human serum albumin(HSA), Pyrimidine derivative, Three dimensional fluorescence technique, Laser flash photolysis, Molecular docking technique

中图分类号:

O623
Q657.3

TrendMD:

唐乾, 苏晋红, 曹洪玉, 王立皓, 史飞, 王爱玲, 宫婷婷, 金晓军, 郑学仿. 嘧啶衍生物与人血清白蛋白的相互作用. 高等学校化学学报, 2017, 38(11): 1982.

TANG Qian, SU Jinhong, CAO Hongyu, WANG Lihao, SHI Fei, WANG Ailing, GONG Tingting, JIN Xiaojun, ZHENG Xuefang. Interaction of Pyrimidine Derivatives with Human Serum Albumin^†. Chem. J. Chinese Universities, 2017, 38(11): 1982.

图/表 15

参考文献 43

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PDs	IC₅₀/(μmol·L^-1)		PDs	IC₅₀/(μmol·L^-1)
PDs	HCC(7721)		MC(A375)	HCC(7721)	MC(A375)
A	23.65	9.42	E	166.90	28.94
B	88.05	81.37	F	22.43	12.85
C	9.53	17.86	G	23.57	27.28
D	16.66	34.76	H	12.22	48.19

PDs	IC₅₀/(μmol·L^-1)		PDs	IC₅₀/(μmol·L^-1)
PDs	HCC(7721)		MC(A375)	HCC(7721)	MC(A375)
A	23.65	9.42	E	166.90	28.94
B	88.05	81.37	F	22.43	12.85
C	9.53	17.86	G	23.57	27.28
D	16.66	34.76	H	12.22	48.19

PDs	T/K	K_SV/ (L·mol^-1)	K_q/ (L·mol^-1·s^-1)	Quenching mechanism	PDs	T/K	K_SV/ (L·mol^-1)	K_q/ (L·mol^-1·s^-1)	Quenching mechanism
A	300	3.206×10⁴	3.20×10¹²	Static quenching	E	300	3.32×10³	3.32×10¹¹	Static quenching
	310	3.17×10⁴	3.17×10¹²			310	6.80×10³	6.80×10¹¹
	320	3.05×10³	3.05×10¹²			320	6.12×10³	6.12×10¹¹
B	300	7.05×10³	7.05×10¹¹	Static quenching	F	300	5.01×10³	5.01×10¹¹	Dynamic quenching
	310	6.82×10³	6.82×10¹¹			310	3.32×10³	3.32×10¹¹
	320	6.36×10³	6.36×10¹¹			320	3.69×10³	3.69×10¹¹
C	300	4.73×10⁴	4.73×10¹²	Static quenching	G	300	4.91×10³	4.91×10¹¹	Dynamic quenching
	310	4.34×10⁴	4.34×10¹²			310	5.65×10³	5.65×10¹¹
	320	3.71×10⁴	3.71×10¹²			320	6.60×10³	6.60×10¹¹
D	300	4.76×10³	4.76×10¹¹	Static quenching	H	300	4.27×10³	4.27×10¹¹	Dynamic quenching
	310	4.40×10³	4.40×10¹¹			310	4.42×10³	4.42×10¹¹
	320	4.20×10³	4.20×10¹¹			320	4.72×10³	4.72×10¹¹

PDs	T/K	K_SV/ (L·mol^-1)	K_q/ (L·mol^-1·s^-1)	Quenching mechanism	PDs	T/K	K_SV/ (L·mol^-1)	K_q/ (L·mol^-1·s^-1)	Quenching mechanism
A	300	3.206×10⁴	3.20×10¹²	Static quenching	E	300	3.32×10³	3.32×10¹¹	Static quenching
	310	3.17×10⁴	3.17×10¹²			310	6.80×10³	6.80×10¹¹
	320	3.05×10³	3.05×10¹²			320	6.12×10³	6.12×10¹¹
B	300	7.05×10³	7.05×10¹¹	Static quenching	F	300	5.01×10³	5.01×10¹¹	Dynamic quenching
	310	6.82×10³	6.82×10¹¹			310	3.32×10³	3.32×10¹¹
	320	6.36×10³	6.36×10¹¹			320	3.69×10³	3.69×10¹¹
C	300	4.73×10⁴	4.73×10¹²	Static quenching	G	300	4.91×10³	4.91×10¹¹	Dynamic quenching
	310	4.34×10⁴	4.34×10¹²			310	5.65×10³	5.65×10¹¹
	320	3.71×10⁴	3.71×10¹²			320	6.60×10³	6.60×10¹¹
D	300	4.76×10³	4.76×10¹¹	Static quenching	H	300	4.27×10³	4.27×10¹¹	Dynamic quenching
	310	4.40×10³	4.40×10¹¹			310	4.42×10³	4.42×10¹¹
	320	4.20×10³	4.20×10¹¹			320	4.72×10³	4.72×10¹¹

Sample	τ₁/ns	τ₂/ns	B₁	B₂	τ/ns	χ²	k₂	C₂/(mol·L^-1)
HSA	2.24	6.62	-0.30	0.81	7.25	1.13	1.51×10⁵	1.59×10^-6
HSA+A	2.18	6.61	-0.37	0.95	7.26	1.25	1.51×10⁵	1.64×10^-6
HSA+B	2.22	6.52	-0.38	0.97	7.18	0.97	1.53×10⁵	1.64×10^-6
HSA+C	2.06	5.58	-0.24	0.59	6.20	1.02	1.79×10⁵	1.69×10^-6
HSA+D	2.26	6.62	-0.39	0.96	7.32	1.26	1.51×10⁵	1.68×10^-6
HSA+E	1.92	5.92	-0.26	0.72	6.45	0.69	1.69×10⁵	1.57×10^-6
HSA+F	1.89	6.00	-0.36	1.05	6.50	1.69	1.67×10⁵	1.52×10^-6
HSA+G	2.00	5.83	-0.43	1.07	6.44	1.25	1.72×10⁵	1.67×10^-6
HSA+H	2.05	6.09	-0.52	1.29	6.72	1.80	1.64×10⁵	1.68×10^-6

嘧啶衍生物与人血清白蛋白的相互作用

Interaction of Pyrimidine Derivatives with Human Serum Albumin^†

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Sample	F₀/F	τ₀/τ	Sample	F₀/F	τ₀/τ
HSA+A	1.13	1.00	HSA+E	3.89	1.12
HSA+B	1.28	1.01	HSA+F	1.11	1.12
HSA+C	2.68	1.18	HSA+G	1.13	1.13
HSA+D	1.18	0.99	HSA+H	1.09	1.08

PDs	T/K	K_a/(L·mol^-1)	n	ΔH/(kJ·mol^-1)	ΔS/(J·mol^-1·K^-1)	ΔG/(kJ·mol^-1)	Interaction force
A	300	3.41×10³	1	-6.62	-45.6	-20.3	Hydrogen bond and Van der
	310	3.17×10³	1.01			-20.76	Waals’ force
	320	2.89×10³	1.02			-21.23
B	300	5.54×10³	1.06	-9.58	39.92	-21.56	Static electricity and
	310	5.22×10³	1.06			-21.96	hydrophobic interaction
	320	4.37×10³	1.09			-22.35
C	300	2.37×10⁴	1.16	-1.37	79.18	-25.12	Static electricity and
	310	2.33×10⁴	1.15			-25.92	hydrophobic interaction
	320	2.29×10⁴	1.11			-26.71
D	300	4.67×10³	0.87	-24.32	-9.98	-21.33	Hydrogen bond and
	310	4.57×10³	1.02			-21.23	Van der Waals’ force
	320	2.57×10³	1.03			-21.13
E	300	1.17×10⁵	0.86	-32.18	9.78	-29.25	Static electricity and
	310	9.07×10⁴	0.90			-29.15	hydrophobic interaction
	320	5.25×10⁴	0.98			-29.05

HSA+PDs	J/(cm³·L·mol^-1)	R₀/nm	E	r/nm
HSA+A	1.55×10^-14	2.64	0.12	3.68
HSA+B	1.43×10^-14	2.60	0.22	3.21
HSA+C	2.95×10^-14	2.94	0.65	2.65
HSA+D	1.41×10^-14	2.60	0.16	3.42
HSA+E	2.54×10^-14	2.86	0.74	2.41

System	Rayleigh scattering peak(Peak 1)			Fluorescence peak(Peak 2)
System	Peak position λ_ex/λ_em(nm/nm)	Stokes Δλ/nm	Fluorescence intensity	Peak position λ_ex/λ_em(nm/nm)	Stokes Δλ/nm	Fluorescence intensity
HSA	290/290	0	134.15	290/334	44	75.80
HSA+A	290/290	0	100.69	290/338	48	51.63
HSA+B	290/290	0	9.22	290/334	44	66.10
HSA+C	290/290	0	112.33	290/328	38	41.25
HSA+D	290/290	0	97.86	290/335	45	67.90
HSA+E	290/290	0	125.45	290/335	45	71.71

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嘧啶衍生物与人血清白蛋白的相互作用

Interaction of Pyrimidine Derivatives with Human Serum Albumin†

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Interaction of Pyrimidine Derivatives with Human Serum Albumin^†