Effects of Hydroxypropyl-β-cyclodextrin(HPCD) on the Interaction of 1-Hydroxypyrene with Bovine Serum Albumin†

doi:10.7503/cjcu20160514

Abstract

Abstract:

Fluorescence spectra, circular dichroism spectra and UV visible absorption spectra were employed to investigate the feasibility of regulating the interaction of 1-hydroxypyrene(1-OHPyr) with bovine serum albumin(BSA) using hydroxypropyl-β-cyclodextrin(HPCD) under simulated physiological conditions, and the related mechanism was preliminary discussed. The results showed that HPCD can inhibit the interaction of 1-OHPyr with BSA, and the binding constant of 1-OHPyr-BSA was decreased to 1.45×10⁵ L/mol at 291 K. HPCD can also restore the helix of BSA and inhibit the polarity changes of the local microenvironment of tryptophan(TRP) residues in BSA. HPCD can increase the fluorescence lifetimes of 1-OHPyr and BSA in 1-OHPyr-BSA system, meanwhile increase the binding distance of 1-OHPyr with BSA. The inclusion behavior of HPCD with 1-OHPyr was primarily the main reason why HPCD affected the binding of 1-OHPyr with BSA.

Key words: 1-Hydroxypyrene, Bovine serum albumin, Hydroxypropyl-β-cyclodextrin, Spectroscopic method, Influencing mechanism

CLC Number:

O657
O625

TrendMD:

ZHANG Jing, CHEN Linfeng, ZHU Yaxian, ZHANG Yong. Effects of Hydroxypropyl-β-cyclodextrin(HPCD) on the Interaction of 1-Hydroxypyrene with Bovine Serum Albumin^†[J]. Chem. J. Chinese Universities, 2017, 38(1): 28.

Figures/Tables 10

Fig.1 Fluorescence emission spectra of 1-OHPyr-BSA system in the presence of HPCD105 c(1-OHPyr)/(mol·L-1), a—f: 0, 0.2, 0.4, 0.5, 0.6, 0.8, 1.0; c(BSA)=1.0×10-6 mol/L; c(HPCD)=3.0×10-3 mol/L, 291 K. (A) Ex. slit: 1 nm; Em. slit: 1 nm; (B) Ex. slit: 2 nm; Em. slit: 2 nm.

Fig.2 Stern-Volmer plot(A) and double logarithm plot(B) for the quenching of BSA by 1-OHPyr in the presence of HPCD

Fig.3 Effects of HPCD on the synchronous fluorescence spectra of 1-OHPyr-BSA systemΔλ=60 nm; c(BSA)=5.0×10-6 mol/L; 105 c(1-OHPyr)/(mol·L-1): a. 0; b. 0.5; c. 1.0. c(HPCD)=3.0×10-3 mol/L.

Table 1 Effects of HPCD on the characteristics of BSA synchronous fluorescence peak in 1-OHPyr-BSA system*

c(1-OHPyr)/(mol·L^-1)	1-OHPyr-BSA		1-OHPyr-BSA-HPCD
c(1-OHPyr)/(mol·L^-1)	λ_max/nm	F/a.u.	λ_max/nm	F/a.u.
0	282	1.58×10⁶	282	1.54×10⁶
1.0×10^-6	284	1.15×10⁶	284	1.27×10⁶
5.0×10^-6	285	7.43×10⁵	285	9.27×10⁶
1.0×10^-5	286	4.32×10⁵	285	6.25×10⁶

Fig.4 CD spectra of the 1-OHPyr-BSA systems with different concentrations of HPCDc(BSA)=4.0×10-8 mol/L; c(1-OHPyr)=4.0×10-7 mol/L; c(HPCD): a. 3.0×10-5 mol/L; b. 3.0×10-4 mol/L.

Table 2 Secondary structural contents of BSA in different systems

System	α-Helix(%)	β-Sheet(%)	Turn(%)	Random coil(%)	NRMSD^a
BSA	50.9	11.6	13.1	24.5	0.101
1-OHPyr-BSA	54.5	8.2	14.6	22.7	0.083
1-OHPyr-BSA-HPCD^b	53.6	11.0	8.9	26.6	0.471
1-OHPyr-BSA-HPCD^c	51.8	10.2	12.0	26.1	0.094

Fig.5 Fluorescence decay curves for 1-OHPyr (A) and BSA (B) in different systems(A) λex=346 nm, λem=386 nm; (B) λex=282 nm, λem=341 nm; c(BSA)=c(1-OHPyr)=5.0×10-6 mol/L; c(HPCD)=3.0×10-3 mol/L.

Table 3 Fluorescence decay parameters for BSA and 1-OHPyr in different systems at 291 K*

System	τ_f(1-OHPyr)/ns	χ²	System	τ_f(BSA)/ns	χ²
1-OHPyr	14.73	1.066	BSA	5.98	1.051
1-OHPyr-HPCD	18.04	1.069	BSA-HPCD	6.06	1.157
1-OHPyr-BSA	16.21	1.070	1-OHPyr-BSA	4.59	1.024
1-OHPyr-BSA-HPCD	17.01	0.997	1-OHPyr-BSA-HPCD	5.07	1.117

Fig.6 Overlap of UV-Vis absorption spectrum of 1-OHPyr(a) in the presence of HPCD with the fluorescence emission spectrum of BSA(b)c(BSA)=c(1-OHPyr)=5.0×10-6 mol/L; c(HPCD)=3.0×10-3 mol/L.

Table 4 Energy transfer parameters between 1-OHPyr and BSA in the absence and presence of HPCD*

System	J/(cm³·L·mol^-1)	E(%)	R₀/nm	r/nm
1-OHPyr-BSA^[6]	1.37×10^-14	40	2.69	2.88
1-OHPyr-BSA-HPCD	2.16×10^-14	21	2.85	3.55

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