Chemical modifications influence the structural stability, lipid binding, and amyloidogenic properties of human serum amyloid A

Abstract Human serum amyloid A (SAA) is an apolipoprotein that predominantly associates with high-density lipoprotein (HDL) in the blood and participates in lipid metabolism. In addition, SAA serves as a precursor of amyloid fibrils that contribute to the development of AA amyloidosis. Chemical modifications of amyloidogenic proteins can influence the formation of amyloid fibrils. Recently, various modified SAA molecular species have been discovered in patients with AA amyloidosis. In the presen