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The structural stability of protein antigens adsorbed by aluminium hydroxide in comparison to the antigens in solutions
Author(s) -
Yiwu Zheng,
Xuxin Lai,
Henrik Ipsen,
Jørgen Nedergaard Larsen,
Henning Løwenstein,
Ib Søndergaard,
Susanne Jacobsen
Publication year - 2007
Publication title -
journal of spectroscopy
Language(s) - English
Resource type - Journals
eISSN - 2314-4920
pISSN - 2314-4939
DOI - 10.1155/2007/354959
Subject(s) - aluminium hydroxide , adsorption , antigen , immunogenicity , chemistry , hydroxide , bovine serum albumin , fourier transform infrared spectroscopy , attenuated total reflection , aluminium , infrared spectroscopy , chemical engineering , biochemistry , inorganic chemistry , biology , immunology , organic chemistry , engineering
It is believed that antigens should be adsorbed onto adjuvants in vaccines. The adsorption-modified structure of antigens is important to understand the mechanism of adjuvants and vaccine immunogenicity. The structural stability of antigens is of major importance. The changes in structure can be induced by degradation and/or increase of storage temperature. In this study the structural stability of two model antigens, bovine serum albumin (BSA) and β-lactoglobulin (BLG) were compared when they were adsorbed onto aluminium hydroxide and when they were in solutions using Fourier transform infrared - attenuated total reflection (FTIR-ATR) spectroscopy. The structural stability of these two proteins was studied at different temperature and during storages. The present results showed that the structure of antigens can be stabilized by adsorption onto aluminium hydroxide. Non-adsorbed protein antigens present in vaccines may facilitate the degradation of the vaccine.

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