Using Sugar-Derived Nanoparticles to Mitigate Amyloid Fibril Formation of Lysozyme

Background: Amyloid fibrils are associated with various degenerative diseases. Considerable efforts have been made to hunt for the compounds that are able to inhibit amyloid fibrillogenesis or disintegrate the mature fibrils. Evidence suggests that interfering with the pathology-associated amyloid fibril formation by small molecules (e.g., osmolytes) or nanoparticles is envisaged as an effective therapeutic strategy. Methods: Amyloid fibrils derived from lysozyme were produced at pH 2.0 and 55 degrees C. Sugar-terminated nanoparticles were prepared via the carbonization of ribose or galactose. Anthrone test was used to determine the surface sugar concentrations on the nanoparticles, and electron microscopy, dynamic light scattering, and spectroscopic techniques were employed to characterize the nanoparticles. The influence of sugar-based nanoparticles on lysozyme fibrillogenesis was investigated via ThT binding assay and electron microscopy. Moreover, the changes of aggregation level and structure in lysozyme samples without and with sugar-terminated nanoparticles were examined. Significant Findings: In contrast to ribose/galactose molecules, ribose-/galactose terminated nanoparticles were found to dose-dependently suppress lysozyme fibrillogenesis. Additionally, decreased aggregation was detected in lysozyme samples upon the addition of either sugar-terminated nanoparticle. Moreover, the estimation of thermodynamic parameters using the fluorescence quenching data revealed that the binding between lysozyme and nanoparticles is mainly governed by the hydrophobic interaction(s). (c) 2022 Taiwan Institute of Chemical Engineers. Published by Elsevier B.V. All rights reserved.