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

doi:10.7503/cjcu20150044

Abstract

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

CLC Number:

O614.37

TrendMD:

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^†[J]. Chem. J. Chinese Universities, 2015, 36(6): 1033.

Figures/Tables 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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