Effects Of Temperature, PH On Sodium Chloride Induced Aggregation Of Lysozyme And The Correlated Mechanism

Over 40 human diseases, including Aβpeptides in Alzheimer’s disease, the PrP prion protein in Creutzfeldt -Jakob, were associated with the deposition of protein fibrils in various organs. The mechanism was not clear. The formation of amyloid was associated with the special structure. And more importantly, the formation was promted under special conditions. The protein could be stable under equilibrium conditions. The presence of any additional ions in solvent might promoted the aggregation.So far, it was reported that 4 lysozyme variants were related to kidney/liver spleen systemic amyloidosis diseases. Hen lysozyme was also closely related to human lysozyme, the variants of which were shown to form amyloid fibrils that were related to hereditary systemic amyloidosis. Hen lysozyme was widely used as a model of human lysozyme.The results of SDS-PAGE showed that both higher temperature and low pH could promote the aggregation of lysozyme. The simulation results indicated that the structure of lysozyme became unstable and moreα-helix conversed toβ-sheet, acompany with temperature increasing, and the disulfide bond Cys76-Cys94 became weaker as temperature increased. Hen lysozyme could be unstable and moreα-helix conversed toβ-sheet at lower pH. The disulfide bond Cys76-Cys94 became weaker at acid condition...