Effects of Gold Nanospheres and Nanocubes on Amyloid-β Peptide Fibrillation
Direct exposure or intake of engineered nanoparticles (ENPs) to the human body will trigger a series of complicated biological consequences. Especially, ENPs could either up- or downregulate peptide fibrillation, which is associated with various degenerative diseases like Alzheimer's and Parkin...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 35(2019), 6 vom: 12. Feb., Seite 2334-2342 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2019
|
| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amyloid beta-Peptides Peptide Fragments amyloid beta-protein (1-40) Gold 7440-57-5 |
| Zusammenfassung: | Direct exposure or intake of engineered nanoparticles (ENPs) to the human body will trigger a series of complicated biological consequences. Especially, ENPs could either up- or downregulate peptide fibrillation, which is associated with various degenerative diseases like Alzheimer's and Parkinson's diseases. This work reports the effects of gold nanoparticles (AuNPs) with different shapes on the aggregation of an amyloid-β peptide (Aβ(1-40)) involved in Alzheimer's disease. Two kinds of AuNPs were investigated, i.e., gold nanospheres (AuNSs, ∼20 nm in diameter) and gold nanocubes (AuNCs, ∼20 nm in edge length). It was found that AuNPs play a catalytic role in peptide nucleation through interfacial adsorption of Aβ(1-40). AuNSs with hybrid facets have higher affinity to Aβ(1-40) because of the higher degree of surface atomic unsaturation than the {100}-faceted AuNCs. Therefore, AuNSs exert a more significant acceleration effect on the fibrillation process of Aβ(1-40) than AuNCs. Besides, a shape-dependent secondary structure transformation of Aβ(1-40) with different AuNPs was observed using Fourier transform infrared spectroscopy. The variation of peptide-NP and peptide-peptide interactions caused by the shape alteration of AuNPs influences the equilibrium of inter- and intramolecular hydrogen bonds, which is believed to be responsible for the shape-dependent secondary structure transformation. The study offers further understanding on the complicated NP-mediated Aβ aggregation and also facilitates further development on designing and synthesizing task-specific AuNPs for amyloid disease diagnosis and therapy |
|---|---|
| Beschreibung: | Date Completed 03.06.2020 Date Revised 03.06.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.8b04006 |