Amyloid fibrillogenesis of proteins have been considered as the major cause behind several degenerative diseases. Nanoparticles have been found to have great potential as a substrate for designing amyloid fibril inhibitors and/or modulators. This is mainly due to its ideal characteristics, such as small size, high surface area-to volume ratio, and modifiable surface. This study is aimed at examining the influence of amino acid-modified silver nanoparticles on amyloid fibril formation. We first synthesized and characterized the proline- and cysteine-functionalized silver nanoparticles (Pro-AgNP and Cys-AgNP). Next, the effects of functionalized silver nanoparticles on amyloid ﬁbrillogenesis and structural changes of hen lysozyme were examined using various spectroscopic and biophysical tools. Our results showed that Pro-AgNP/Cys-AgNP dose-dependently suppressed lysozyme amyloid fibrillogenesis, whereas negligible fibril-inhibiting effect was observed in the bare AgNP or proline/cysteine. Moreover, reduced solvent exposure and α-to-β transition were detected in lysozyme upon the addition of Pro-AgNP/Cys-AgNP. Finally, the nature of interactions between lysozyme and Pro-AgNP/Cys-AgNP was further examined using fluorescence quenching and molecular docking. By altering the properties of nanoparticles to design suitable nanoprobes, we have shown that amyloid fibrillogenesis can be controlled.
|期刊||Colloids and Surfaces B: Biointerfaces|
|出版狀態||已發佈 - 2023 2月|
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