牛血清白蛋白淀粉样纤维化及其细胞毒性

More than 20 human diseases have been reported to be associated with the conversion of proteins and peptides into amyloid fibrils. However, the molecular mechanism of the amyloid formation and the fibrillar cytotoxicity are still unclear and kept to be further explored. In the present study, bovine serum albumin (BSA), a non-pathogenic protein, has been investigated in the terms of amyloid formation and fibrillar cytotoxicity. The results indicated that BSA assemblied into amyloid fibrils by incubating the protein at pH 7.4 and 65°C. The BSA amyloid fibrils were characterized by ThT fluorescence, circular dichroism and TEM images. ANS fluorescence data indicated that the hydrophobicity of BSA fibrillar surface was low and therefore lacked the ability to induce hemolysis of red blood cells. We concluded that a protein with high molecular weight such as BSA can also form amyloid fibrils, although the resultant BSA amyloids showed no cytotoxicity due mainly to their low surface hydrophobicity.