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Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-L-cysteine capped quantum dots.

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TLDR
It is demonstrated that the amyloid fibrillation can be inhibited by quenching the nucleation and elongation processes with a low concentration of water dispersed N-acetyl-L-cysteine capped quantum dots (NAC-QDs).
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This article is published in Biomaterials.The article was published on 2010-01-01. It has received 126 citations till now. The article focuses on the topics: Amyloid & Fibril.

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Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

TL;DR: This review will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality.
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Molecular Interaction of Proteins and Peptides with Nanoparticles

TL;DR: This review summarizes recent progress in understanding the molecular mechanisms of the interactions between proteins or peptides and NPs in order to predict the structural, functional, and/or nanotoxic consequences of these interactions.
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Elevation of Glutathione as a Therapeutic Strategy in Alzheimer Disease

TL;DR: This review focuses on the elevation on glutathione through N-acetyl-cysteine (NAC) and γ-glutamyl Cysteine ethyl ester (GCEE) as a potential therapeutic approach for Alzheimer disease.
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Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: functional similarities with proteins.

TL;DR: It is reported that model CdTe nanoparticles (NPs) can efficiently prevent fibrillation of Aβ associating with 100–330 monomers at once, and this data suggest that inorganic NPs can mimic some sophisticated biological functionalities of proteins.
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Biosafety and Bioapplication of Nanomaterials by Designing Protein–Nanoparticle Interactions

TL;DR: In this article, the current understanding of protein-NP interactions is summarized, including the theoretical background, experimental results, and computational progresses, along with future directions and challenges in this exciting field.
References
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Journal ArticleDOI

Experimental Determination of the Extinction Coefficient of CdTe, CdSe, and CdS Nanocrystals

TL;DR: In this article, the extinction coefficient per mole of nanocrystals at the first exitonic absorption peak, e.g., for high-quality CdTe, CdSe, and CdS, was found to be strongly dependent on the size of the nanocrystal, between a square and a cubic dependence.
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Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?

TL;DR: It is proposed that this step is mechanistically relevant to amyloid formation in human prion disease and in AD; it is the formation of an ordered nucleus, which is the defining characteristic of a nucleation-dependent polymerization.
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Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders.

TL;DR: Recent biophysical studies aimed at elucidating the precise mechanism of in vitro aggregation and animal modeling studies support the emerging notion that an ordered prefibrillar oligomer, or protofibril, may be responsible for cell death and that the fibril form that is typically observed at autopsy may actually be neuroprotective.
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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.

TL;DR: Fluorescence intensity in the presence of a constant amount of amyloid fibrils reached a plateau with increase in the thioflavine T concentration, and the fluorescence was considerably diminished when structure of the amyloids fibril was disrupted by guanidine-HCl treatment.
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Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism

TL;DR: The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions.
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