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Journal of Chemistry
Volume 2013, Article ID 583148, 7 pages
Research Article

Study on the Interaction between Cadmium Sulphide Nanoparticles and Proteins by Resonance Rayleigh Scattering Spectra

1Department of Chemistry and Life Science, Hechi University, Yizhou, Guangxi 546300, China
2Research Center for Analysis and Measurement, Kunming University of Science and Technology, Kunming 650093, China
3Kunming Dihon Pharmaceutical Co., Ltd., Kunming 650000, China

Received 29 June 2013; Revised 31 October 2013; Accepted 14 November 2013

Academic Editor: Roberto Comparelli

Copyright © 2013 Weiwei Zhu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The interaction of cadmium sulphide nanoparticles 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 with to 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 ( ) is directly proportional to the concentration of proteins. A new RRS method for the determination of trace proteins using uncapped nanoparticles 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.