Spectroscopy and Spectral Analysis, Volume. 32, Issue 8, 2166(2012)

Interaction between Latex Microspheres and Antibody Proteins Revealed by Fluorescence Spectroscopy

YU Si-ming1、*, PENG Yun-ping1,2, YU Shu-juan1, LV Huan1, and GUO Cheng1
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  • 1[in Chinese]
  • 2[in Chinese]
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    Latex-antibody complexes were prepared by the method of covalent coupling and the properties of the complexes were studied by fluorescence spectrophotometric method for the purpose of revealing the interaction between latex microspheres and antibody proteins. Analysis of intrinsic fluorescence spectra showed that after being coupled with latex microspheres, the emission maximum of antibody protein showed an obvious blue shift, the intensity of emission maximum decreased significantly, the tertiary structure of antibody protein changed to some extent, the interaction between latex microspheres and antibody proteins had a great quenching effect on the intrinsic fluorescence spectra of antibody proteins, the quenching effect was enhanced along with the increasing pH value and latex concentration, and the quenching mechanism was static quenching. Results of exogenous fluorescence spectra showed that the fluorescence intensity of emission maximum was enhanced significantly after being coupled with latex microspheres, the hydrophobicity of antibody protein was decreasing with the increase in the pH values, however, due to the increasing latex concentration, the hydrophobicity antibody protein was increasing.

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    YU Si-ming, PENG Yun-ping, YU Shu-juan, LV Huan, GUO Cheng. Interaction between Latex Microspheres and Antibody Proteins Revealed by Fluorescence Spectroscopy[J]. Spectroscopy and Spectral Analysis, 2012, 32(8): 2166

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    Paper Information

    Received: Feb. 23, 2012

    Accepted: --

    Published Online: Sep. 26, 2012

    The Author Email: Si-ming YU (tayiya@126.com)

    DOI:10.3964/j.issn.1000-0593(2012)08-2166-05

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