ABSTRACT
Amyloid fibrils, which are formed from aggregates of aberrant proteins, can cause various forms of amyloidosis (including Alzheimer's disease). Such disorders often occur in elderly populations and are suspected to be lifestyle related. Thus, it has been speculated that some foodstuffs could be beneficial for preventing amyloidosis. In this study, we determine whether fibril formation by the hen egg white lysozyme (HEWL) could be inhibited by conducting a thioflavin T assay followed by fluorescence and electron microscopy observations. The results demonstrated that four peptide specimens prepared by the hydrolysis of crude proteins from the egg white, egg yolk, chalazae, and eggshell membrane of hen eggs effectively inhibited HEWL fibril formation. Among the four specimens, peptides from chalazae exhibited the highest preventive ability. The superiority of chalaza peptides was also observed when fibril formation was assayed using a full-length human lysozyme and human amyloid ß peptide 1-42, which is the key factor for the development of Alzheimer's disease. Our study of the fibrillization of the human lysozyme also showed that metal ions (Zn2+, Ca2+, Co2+, Mn2+ and Al3+) promoted fibrillization, and their effects were abolished by the peptide specimens (especially by chalaza peptides). Thus, we conclude that chicken-egg proteins could be a convenient source of therapeutic materials for amyloidosis.
ABSTRACT
It is of interest to determine whether and how egg-white proteins are maintained in fertile eggs. We previously observed that egg-white ovalbumin attained high stability during embryogenesis. Herein, we observed that the total mass of egg white and that of its gross protein content showed a decrease according to the days of incubation. The total bacteriolytic activity also lowered, in accord with previous observations. We purified lysozyme from egg-white samples on several incubation days. These purified lysozyme proteins were observed to have enzymatic and bacteriolytic activities against Micrococcus lysodeikticus as well as growth-inhibition potency against Staphylococcus aureus. As the embryogenesis proceeded, the purified lysozyme showed changes in Km and Vmax, a small decrease in the denaturation temperature, and symptoms of an increase in surface hydrophobicity. These results indicate that the lysozyme protein maintained its enzymatic and antibacterial activities until the late period of incubation while undergoing slight conformational changes.