Abstract
Some natural variants of human lysozyme are associated with systemic non-neurological amyloidosis that leads to amyloid protein fibril deposition in different tissues. Inhibition of amyloid fibrillation by nanomaterials is considered to be an effective approach to treating amyloidosis. Here, we prepared a targeted, highly loaded curcumin lysozyme-imprinted nanosphere (CUR-MIMS) that could effectively inhibit the aggregation of lysozyme with lysozyme adsorption capacity of 193.57 mg g−1 and the imprinting factor (IF) of 3.72. CUR-MIMS could bind to lysozyme through hydrophobic interactions and effectively reduce the hydrophobicity of the total solvent-exposed surface in lysozyme fibrillation, thus reducing the self-assembly process triggered by hydrophobic interactions. Thioflavin T (ThT) analysis demonstrated that CUR-MIMS inhibited the aggregation of amyloid fibrils in a dose-dependent manner (inhibition efficiency of 56.07 %). Circular dichroism (CD) spectrum further illustrated that CUR-MIMS could significantly inhibit the transition of lysozyme from α-helix structure to β-sheet. More importantly, biological experiments proved the good biocompatibility of CUR-MIMS, which indicated the potential of our system as a future therapeutic platform for amyloidosis.
Published Version
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