Gold nanoparticles as amyloid-like fibrillogenesis inhibitors

•Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more c...

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Veröffentlicht in:	Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2013-12, Vol.112, p.525-529
Hauptverfasser:	Hsieh, Shuchen, Chang, Chiung-wen, Chou, Hsuan-hung
Format:	Artikel
Sprache:	eng
Schlagworte:	AFM Alzheimer disease Alzheimer Disease - drug therapy Alzheimer Disease - metabolism Alzheimer's amyloid Amyloid - antagonists & inhibitors Amyloid - chemistry Amyloid - ultrastructure Amyloid fibril amyloidosis Animals Blood-Brain Barrier Brain Cattle Circular Dichroism colloids Diseases Drug Delivery Systems Gold Gold - chemistry Humans hypoglycemic agents Inhibitors Insulin Insulin - chemistry insulin resistance Metal Nanoparticles - chemistry Microscopy, Atomic Force Microscopy, Electron, Transmission nanogold Nanoparticle Nanoparticles Nanostructure patients Protein Multimerization - drug effects therapeutics
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Beschreibung
Zusammenfassung:	•Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more compact. Amyloid aggregates are one of the likely key factors leading to the development of Alzheimer's disease (AD) and other amyloidosis associated diseases. Several recent studies have shown that some anti-diabetic drugs have a positive therapeutic effect on AD patients by crossing the blood brain barrier (BBB) and preventing or reducing insulin resistance. Nanoparticles (NPs) or nanoscale objects (
ISSN:	0927-7765 1873-4367
DOI:	10.1016/j.colsurfb.2013.08.029