Modulation effect of acidulated human serum albumin on Cu2 +-mediated amyloid β-protein aggregation and cytotoxicity under a mildly acidic condition

The research revealed that acidulated human serum albumin (A-HSA) changed the coordination mode of Cu2+ and amyloid β-proteins (Aβ) at pH 6.6, which avoided the formation of aggregation-prone Cu2+-Aβ42 aggregates. Thus, A-HSA worked as a bifunctional inhibitor against Cu2+-Aβ42 aggregation and cytotoxicity under a mildly acidic condition.87