Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots

Xiao, Lehui; Zhao, Dan; Chan, Wing Hong; Choi, Martin M.F.; Li, Hung‐Wing

doi:10.1016/j.biomaterials.2009.09.014

Cited by 131 publications

(101 citation statements)

References 34 publications

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“…In particular, the interaction of various nanoparticles with specific protein aggregates (amyloids) can be mentioned. Among different types of probed materials [35] magnetic nanoparticles of iron oxides show inhibiting and even disaggregating effect on amyloidal aggregation [36][37][38][39][40].…”

Section: Sans Contrast Variationmentioning

confidence: 99%

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Melníková

Петренко

Авдеев

et al. 2014

Colloids and Surfaces B: Biointerfaces

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Synthetic biological macromolecule of magnetoferritin containing an iron oxide core inside a protein shell (apoferritin) is prepared with different content of iron. Its structure in aqueous solution is analyzed by small-angle synchrotron X-ray (SAXS) and neutron (SANS) scattering.The loading factor (LF) defined as the average number of iron atoms per protein is varied up to LF=800. With an increase of the LF, the scattering curves exhibit a relative increase in the total scattered intensity, a partial smearing and a shift of the match point in the SANS contrast variation data. The analysis shows an increase in the polydispersity of the proteins and a corresponding effective increase in the relative content of magnetic material against the protein moiety of the shell with the LF growth. At LFs above ~150, the apoferritin shell undergoes structural changes, which is strongly indicative of the fact that the shell stability is affected by iron oxide presence.

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Section: Sans Contrast Variationmentioning

confidence: 99%

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Melníková

Петренко

Авдеев

et al. 2014

Colloids and Surfaces B: Biointerfaces

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“…The effect of nanoparticles on amyloid formation in proteins has not been determined yet. Several researches show that different size, surface and concentration of nanoparticles affect protein aggregation in different ways [8,9]. Protein aggregation is a problem of current interest because many human diseases are related to protein aggregation [10,11] and various methods have been used to study factors which can influence protein aggregation [12].…”

Section: Introductionmentioning

confidence: 99%

Interaction of Magnetic Nanoparticles with Lyotropic Liquid Crystal Studied by AFM

et al. 2017

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In this work the interaction of lysozyme fibrils with magnetic particles has been studied by atomic force microscopy. The experiments were carried out for a better understanding of the binding process of such complex soft matter systems. The obtained results show that interaction between lysozyme fibrils and magnetic particles starts immediately after mixing them together. Moreover, the samples remain stable in duration of several days after preparation.

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“…Quantum dots (QDs), a class of typical nanoparticles, have been extensively studied with proteins to explore their potential biomedical applications. One study illustrated that N-acetyl-L-cysteine capped CdTeQDs inhibit amyloid beta 1-40 fibril formation in vitro [11]. On the contrary, Page -02…”

Section: Introductionmentioning

confidence: 99%

Dihydrolipoic Acid Conjugated Carbon Dots Accelerate Human Insulin Fibrillation

Kuruvilla¹,

Li²,

Sansalone³

et al. 2015

J Parkinsons Dis Alzheimers Dis

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Protein fibrillation is believed to play an important role in the pathology and development of several human diseases, such as Alzheimer's disease, Parkinson's disease and type 2 diabetes. Carbon dots (CDs), as a new type of nanoparticle have recently been extensively studied for potential biological applications, but their effects on protein fibrillation remain unexplored. In reality, any application in biological systems will inevitably have "contact" between proteins and CDs. In this study, human insulin was selected as a model protein to study the effects of CDs on protein fibrillation, as proteins may share a common mechanism to form fibrils. Hydrophobic CDs were conjugated with dihydrolipoic acid (DHLA-CDs) to facilitate their water solubility. Characterizations from thioflavin T fluorescence, circular dichroism spectroscopy and atomic force microscopy demonstrate that the presence of DHLA-CDs results in a higher rate of human insulin fibrillation, accelerating the conformational changes of human insulin from α-helix to β-sheet. This promoting effect is likely associated with the locally increased concentration of human insulin adsorbed on the surface of DHLA-CDs.

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Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots

Cited by 131 publications

References 34 publications

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Interaction of Magnetic Nanoparticles with Lyotropic Liquid Crystal Studied by AFM

Dihydrolipoic Acid Conjugated Carbon Dots Accelerate Human Insulin Fibrillation

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