Amphiphilic modification of human lysozyme enhances its ability to inhibit Aβ42 aggregation

Abstract

Human lysozyme (hLYZ) was sequentially PEGylated, conjugated with ethylenediamine, and propionylated to yield PEGylated, cationic, and amphiphilic derivatives, respectively. The ability of these derivatives to inhibit amyloid β 42 (Aβ42) aggregation was evaluated and compared with that of unmodified hLYZ. Among the hLYZ derivatives examined, amphiphilic hLYZ showed the strongest inhibition of Aβ42 aggregation. These results suggest that amphiphilic modification of hLYZ through the introduction of polyethylene glycol (PEG) and hydrophobic groups may be a useful strategy for improving its ability to inhibit Aβ42 aggregation.