Affiliations: ALK-ABELLO A/S, Hørsholm, Denmark | Enzyme and Protein Chemistry, BioCentrum-DTU, Technical University of Denmark, Kgs. Lyngby, Denmark
Note: [] Corresponding author: Susanne Jacobsen, Enzyme and Protein Chemistry, BioCentrum-DTU, Technical University of Denmark, Søltofts Plads, Building 224, 2800 Kgs. Lyngby, Denmark. Tel.: +45 4525 2741; Fax: +45 4588 6307; E-mail: sja@biocentrum.dtu.dk.
Abstract: 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.
