The investigation of the interactions between CdSe quantum dots and human serum albumin by resonance Rayleigh scattering and second-order scattering spectra

Author(s):  
Ke-Jing Huang ◽  
Cai-Yun Wei ◽  
Yan-Mei Shi ◽  
Wan-Zhen Xie ◽  
Wei Wang
Luminescence ◽  
2012 ◽  
Vol 28 (6) ◽  
pp. 842-846 ◽  
Author(s):  
Shengmian Wang ◽  
Lili Xu ◽  
Lisheng Wang ◽  
Aihui Liang ◽  
Zhiliang Jiang

2013 ◽  
Vol 2013 ◽  
pp. 1-7
Author(s):  
Weiwei Zhu ◽  
Qi Wang ◽  
Dan Su

The interaction of cadmium sulphide nanoparticles[(CdS)n]with proteins has been studied by resonance Rayleigh scattering spectra (RRS). Below the isoelectric point, proteins such as bovine serum albumin (BSA), human serum albumin (HSA), lysozyme (Lys), hemoglobin (HGB), and ovalbumin (OVA) can bind withCdSnto form macromolecules by virtue of electrostatic attraction and hydrophobic force. It can result in the enhancement of resonance Rayleigh scattering spectra (RRS) intensity. Their maximum scattering peaks were 280 nm, and there was a smaller peak at 370 nm. The scattering enhancement (ΔIRRS) is directly proportional to the concentration of proteins. A new RRS method for the determination of trace proteins using uncappedCdSnnanoparticles probe has been developed. The detection limits are 19.6 ng/mL for HSA, 16.7 ng/mL for BSA, 18.5 ng/mL for OVA, 80.2 ng/mL for HGB, and 67.4 ng/mL for Lys, separately. In this work, the optimum condition of reaction, the effect of foreign, and the analytical application had been investigated.


2010 ◽  
Vol 104 (11) ◽  
pp. 1148-1155 ◽  
Author(s):  
Jianbo Xiao ◽  
Tingting Chen ◽  
Longsheng Chen ◽  
Hui Cao ◽  
Fan Yang ◽  
...  

1986 ◽  
Vol 29 (1-4) ◽  
pp. 1407-1409 ◽  
Author(s):  
G. Albanese ◽  
A. Deriu ◽  
F. Cavatorta ◽  
V. F. Krupyanskii ◽  
I. P. Suzdalev ◽  
...  

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