LaPO4:Eu fluorescent nanorods, synthesis, characterization and spectroscopic studies on interaction with human serum albumin

被引:7
作者
Guo, Xingjia [1 ]
Yao, Jie [1 ]
Liu, Xuehui [1 ]
Wang, Hongyan [2 ]
Zhang, Lizhi [1 ]
Xu, Liping [1 ]
Hao, Aijun [3 ]
机构
[1] Liaoning Univ, Coll Chem, Shenyang 110036, Liaoning, Peoples R China
[2] Jingzhou Prod Qual Supervis & Testing Inst, Jinzhou 121000, Peoples R China
[3] Liaoning Univ, Coll Pharm, Shenyang 110036, Liaoning, Peoples R China
关键词
LaPO4:Eu; Human serum albumin; Spectroscopic methods; Interaction; MOLECULAR-DYNAMICS SIMULATION; LUMINESCENT PROPERTIES; HYDROTHERMAL SYNTHESIS; BINDING; NANOPARTICLES; DOCKING; ACID; PHOTOLUMINESCENCE; NANOMATERIALS; NANOCRYSTALS;
D O I
10.1016/j.saa.2018.02.066
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Eu3+ doped LaPO4 fluorescent nanorods (LaPO4:Eu) was successfully fabricated by a hydrothermal process. The obtained LaPO4:Eu nanorods under the optimal conditions were characterized by means of transmission electron microscopy (TEM), X-ray diffraction (XRD) technique, Fourier transform infrared (FTIR), UV-vis absorption and fluorescence spectroscopy. The nanorods with a length of 50-100 nm and a diameter of about 10 nm, can emit strong red fluorescence upon excitation at 241 nm. The FTIR result confirmed that there are lots of phosphate groups on the surfaces of nanorods. In order to better understand the physiological behavior of nanorods in human body, multiple spectroscopic methods were used to study the interaction between the LaPO4:Eu nano rods and human serum albumin (HSA) in the simulated physiological conditions. The results indicated that the nanorods can effectively quench the intrinsic fluorescence of HSA through a dynamic quenching mode with the association constants of the order of 10(3) L mol(-1). The values of the thermodynamic parameters suggested that the binding of the nanorods to HSA was a spontaneous process and van der Waals forces and hydrogen bonds played a predominant role. The displacement experiments verified that the binding site of nanorods on HSA was mainly located in the hydrophobic pocket of subdomain IIA (site I) of HSA. The binding distance between nanorods and HSA was calculated to be 4.2 nm according to the theory of Forster non-radiation energy transfer. The analysis of synchronous fluorescence, three-dimensional fluorescence (3D) and circular dichroism (CD) spectra indicated that there the addition of LaPO4:Eu nanorods did not caused significant alterations in conformation of HSA secondary structure and the polarity around the amino acid residues. (C) 2018 Elsevier B.V. All rights reserved.
引用
收藏
页码:248 / 256
页数:9
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