Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1–40) fibrillogenesis

Chan, Ho Man; Xiao, Lehui; Yeung, K. M.; Ho, See Lok; Zhao, Dan; Chan, Wai-Yip; Li, Hung‐Wing

doi:10.1016/j.biomaterials.2012.03.024

Cited by 64 publications

(57 citation statements)

References 30 publications

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“…[21] The ThT fluorescence assay was performed as described previously. [22] PAP 248-286 (2 mg mL À1 ,0 .44 mmol L À1 )w as mixed with brazilin or EGCG at various molar ratios (brazilin/PAP 248-286 ,0 .1-1:1;E GCG/ PAP 248-286 ,0 .1-2:1). The mixtures were incubated at 37 8Cw ith continuous orbital shaking at 1400 rpm.…”

Section: Thioflavin Tf Luorescence Assaysmentioning

confidence: 99%

Brazilin Inhibits Prostatic Acidic Phosphatase Fibrillogenesis and Decreases its Cytotoxicity

Dong

Liu³

et al. 2017

Chemistry An Asian Journal

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A 39-amino acid peptide fragment that is derived from prostatic acidic phosphatase (PAP), PAP , is secreted in large amounts in human semen and forms amyloid fibrils. These fibrils can capture HIV virions and increase the attachment of virions to target cells; as such, they are called a "semen-derived enhancer of virus infection" (SEVI). Therefore, the inhibition of the formation of PAP amyloid fibrils is of great significance. Herein, we demonstrate that brazilin effectively inhibits PAP aggregation. The inhibitory effect increases with increasing brazilin concentration. Thioflavin T fluorescence assays and TEM observations confirmed that a few fibrils formed when brazilin was present with PAP in an equimolar concentration. Circular dichroism spectroscopy indicated that brazilin inhibited the secondary structural transitions from α-helices and random coils into β-sheets. Cytotoxicity assays showed that brazilin significantly decreased the cytotoxicity of the fibrils at 0.01 mmol L . Isothermal titration calorimetry revealed that hydrophobic interactions were the main driving force for the binding of brazilin to the PAP monomer (dissociation constant, 4.03 μmol L ), and that the binding affinity of brazilin for the fibrils was at least three orders of magnitude lower than that for the monomer. These results indicate that brazilin holds great potential as a small-molecule agent against SEVIs.

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Section: Thioflavin Tf Luorescence Assaysmentioning

confidence: 99%

Brazilin Inhibits Prostatic Acidic Phosphatase Fibrillogenesis and Decreases its Cytotoxicity

Dong

Liu³

et al. 2017

Chemistry An Asian Journal

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“…This indicates that the binding of Aβ on SeNPs might affect metal ion induced Aβ aggregation. Evidence shows that binding of nanoparticles to Aβ can be affected by surface modifications, including ligands, charges, or reactivity . Thus, SeNPs with proper surface modifications are expected to improve the binding affinity of SeNPs for Aβ.…”

Section: Introductionmentioning

confidence: 99%

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

Yang

Wang

Chen

et al. 2018

J Biomedical Materials Res

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Deposition of amyloid‐β (Aβ) aggregates and formation of neurotoxic reactive oxygen species (ROS) are significant pathological signatures of Alzheimer's disease (AD). Resveratrol (Res) is an antioxidant with the potential to treat AD. However, the bioavailability and solubility of Res is very low and it cannot entirely inhibit Cu2+‐induced Aβ42 aggregation at low concentration. Herein, we combine the unique Aβ absorption property of selenium nanoparticles with the natural antioxidant agent Res to form Res@SeNPs. Our in vitro biological evaluation revealed that modification of Res with SeNPs provides a synergistic effect on Cu2+‐induced Aβ42 aggregation, ROS generation and, more importantly, protects PC12 cells from Aβ42–Cu2+ complexes‐induced cell death. It is believed that SeNPs can improve the application of Res in AD treatment as Res@SeNPs is more efficient than Res in reducing Aβ42 toxicity in long‐term use. © 2018 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 106A: 3034–3041, 2018.

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“…Such information is not only valuable for design safe and effective nanoparticles, but also investigating the mechanism of protein misfolding disease. If NPs can inhibit the process of the formation of amyloid fibrils, they will have great potential to be used as valuable therapeutic materials to control amyloid diseases like Alzheimer’s disease [31]–[34]. However, if NPs promote the aggregation of peptides or proteins, it will cause toxicity.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Influence of Carbon Nanoparticles on the Formation of β-Sheet-Rich Oligomers of IAPP22–28 Peptide by Molecular Dynamics Simulation

Guo

Zhang

et al. 2013

PLoS ONE

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Recent advances in nanotechnologies have led to wide use of nanomaterials in biomedical field. However, nanoparticles are found to interfere with protein misfolding and aggregation associated with many human diseases. It is still a controversial issue whether nanoparticles inhibit or promote protein aggregation. In this study, we used molecular dynamics simulations to explore the effects of three kinds of carbon nanomaterials including graphene, carbon nanotube and C60 on the aggregation behavior of islet amyloid polypeptide fragment 22–28 (IAPP22–28). The diverse behaviors of IAPP22–28 peptides on the surfaces of carbon nanomaterials were studied. The results suggest these nanomaterials can prevent β-sheet formation in differing degrees and further affect the aggregation of IAPP22–28. The π–π stacking and hydrophobic interactions are different in the interactions between peptides and different nanoparticles. The subtle differences in the interaction are due to the difference in surface curvature and area. The results demonstrate the adsorption interaction has competitive advantages over the interactions between peptides. Therefore, the fibrillation of IAPP22–28 may be inhibited at its early stage by graphene or SWCNT. Our study can not only enhance the understanding about potential effects of nanomaterials to amyloid formation, but also provide valuable information to develop potential β-sheet formation inhibitors against type II diabetes.

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Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1–40) fibrillogenesis

Cited by 64 publications

References 30 publications

Brazilin Inhibits Prostatic Acidic Phosphatase Fibrillogenesis and Decreases its Cytotoxicity

Brazilin Inhibits Prostatic Acidic Phosphatase Fibrillogenesis and Decreases its Cytotoxicity

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

Exploring the Influence of Carbon Nanoparticles on the Formation of β-Sheet-Rich Oligomers of IAPP22–28 Peptide by Molecular Dynamics Simulation

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