LVFFARK-PEG-Stabilized Black Phosphorus Nanosheets Potently Inhibit Amyloid-β Fibrillogenesis

Deposition of amyloid-β (Aβ) aggregates in the brain is a main pathological hallmark of Alzheimer's disease (AD), so inhibition of Aβ aggregation has been considered as a promising strategy for AD prevention and treatment. Black phosphorus (BP) is a 2D nanomaterial with high biocompatibility an...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 36(2020), 7 vom: 25. Feb., Seite 1804-1812
1. Verfasser: Yang, Junnan (VerfasserIn)
Weitere Verfasser: Liu, Wei, Sun, Yan, Dong, Xiaoyan
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
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 Peptides amyloid beta-protein (1-42) Phosphorus 27YLU75U4W Polyethylene Glycols 3WJQ0SDW1A
Beschreibung
Zusammenfassung:Deposition of amyloid-β (Aβ) aggregates in the brain is a main pathological hallmark of Alzheimer's disease (AD), so inhibition of Aβ aggregation has been considered as a promising strategy for AD prevention and treatment. Black phosphorus (BP) is a 2D nanomaterial with high biocompatibility and unique biodegradability, but its potential application in biomedicine suffers from the rapid degradability and unfunctionability. To overcome the drawbacks and broaden its application, we have herein designed an Aβ inhibitor (LK7)-coupled and polyethylene glycol (PEG)-stabilized BP-based nanosystem. The PEGylated-LK7-BP nanosheets (PEG-LK7BP) not only exhibited a good stability but also demonstrated a significantly enhanced inhibitory potency on Aβ42 fibrillogenesis in comparison with its counterparts. This elaborately designed PEG-LK7@BP stopped the conformational transition and suppressed the fibrillization of Aβ42, so it could completely rescue cultured cells from the toxicity of Aβ42 (by increasing the cell viability from 72 to 100%) at 100 μg/mL. It is considered that PEG-LK7@BP could bind Aβ species by enhanced electrostatic and hydrophobic interactions and thus efficiently alleviated Aβ-Aβ interactions. Meanwhile, the coupled LK7 on the BP surface formed a high local concentration that enhanced the affinity between the nanosystem and Aβ species. Finally, PEG could improve the stability and dispersibility of the nanoplatform to make it show an increased inhibitory effect on the amyloid formation. Hence, this work proved that PEG-LK7@BP is a promising nanosystem for the development of amyloid inhibitors fighting against AD
Beschreibung:Date Completed 04.12.2020
Date Revised 14.12.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.9b03612