Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity

Anand, Bibin G.; Wu, Qi; Karthivashan, Govindarajan; Shejale, Kiran P.; Amidian, Sara; Wille, Holger; Kar, Satyabrata

doi:10.1016/j.bioactmat.2021.04.029

Cited by 24 publications

(18 citation statements)

References 78 publications

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“…A small aliquot (10 μl) of Aβ 1–42 and Aβ 42–1 sample in absence and presence of different concentrations of PLGA was added separately on a clean glass slide, air-dried and then stained with ThT solution as described earlier [ 45 ]. The images of ThT-stained Aβ 1–42 and Aβ 42–1 aggregates were then captured using a fluorescence microscope (Nikon eclipse 90i) at 20X magnification.…”

Section: Methodsmentioning

confidence: 99%

“…The size distribution of aggregated Aβ 1–42 samples in the absence or presence of PLGA, PEG-PLGA and PCL, at the end of the lag phase and/or after reaching saturation (i.e., 24 h), were carried out with a Malvern Zetasizer-Nano Instrument as described earlier [ 45 ]. A He–Ne laser with a wavelength of 632 nm was used to detect backscattered light at a fixed angle of 173°.…”

Section: Methodsmentioning

confidence: 99%

“…The viability of control and treated neurons following various experimental paradigms was determined using the MTT and/or LDH assays as previously described [ 44 , 45 ]. For the MTT assay, the culture media of the neurons was replaced with new media containing 0.5 mg/ml MTT, the cells were incubated for 4 h at 37 °C, the formazan crystals were dissolved in dimethyl sulfoxide and absorbance was measured at 570 nm with a microplate reader.…”

Section: Methodsmentioning

confidence: 99%

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Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology

Paul

Cho

et al. 2022

J Nanobiotechnol

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Conversion of β-amyloid (Aβ) peptides from soluble random-coil to aggregated protein enriched with β-sheet-rich intermediates has been suggested to play a role in the degeneration of neurons and development of Alzheimer’s disease (AD) pathology. Aggregation of Aβ peptide can be prompted by a variety of environmental factors including temperature which can influence disease pathogenesis. Recently, we reported that FDA-approved unconjugated poly (d,l-lactide-co-glycolide) (PLGA) nanoparticles can have beneficial effects in cellular and animal models of AD by targeting different facets of the Aβ axis. In this study, using biochemical, structural and spectroscopic analyses, we evaluated the effects of native PLGA on temperature-dependent Aβ aggregation and its ability to protect cultured neurons from degeneration. Our results show that the rate of spontaneous Aβ1–42 aggregation increases with a rise in temperature from 27 to 40 °C and PLGA with 50:50 resomer potently inhibits Aβ aggregation at all temperatures, but the effect is more profound at 27 °C than at 40 °C. It appears that native PLGA, by interacting with the hydrophobic domain of Aβ1–42, prevents a conformational shift towards β-sheet structure, thus precluding the formation of Aβ aggregates. Additionally, PLGA triggers disassembly of matured Aβ1–42 fibers at a faster rate at 40 °C than at 27 °C. PLGA-treated Aβ samples can significantly enhance viability of cortical cultured neurons compared to neurons treated with Aβ alone by attenuating phosphorylation of tau protein. Injection of native PLGA is found to influence the breakdown/clearance of Aβ peptide in the brain. Collectively, these results suggest that PLGA nanoparticles can inhibit Aβ aggregation and trigger disassembly of Aβ aggregates at temperatures outside the physiological range and can protect neurons against Aβ-mediated toxicity thus validating its unique therapeutic potential in the treatment of AD pathology. Graphical Abstract

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology

Paul

Cho

et al. 2022

J Nanobiotechnol

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“…Small molecules and peptides can be conjugated on the surface of nanomaterials to improve the properties and efficiency of both the modifiers and the nanomaterials [ 47 ]. For example, Palmal et al prepared curcumin-functionalized AuNPs and found that water-soluble AuNPs with multiple curcumin moieties on the surface could inhibit Aβ fibrillation and dissolve Aβ fibrils without using other external agent or force [ 48 ].…”

Section: Nanomaterialsmentioning

confidence: 99%

Nanomaterials for Modulating the Aggregation of β-Amyloid Peptides

et al. 2021

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The aberrant aggregation of amyloid-β (Aβ) peptides in the brain has been recognized as the major hallmark of Alzheimer’s disease (AD). Thus, the inhibition and dissociation of Aβ aggregation are believed to be effective therapeutic strategiesforthe prevention and treatment of AD. When integrated with traditional agents and biomolecules, nanomaterials can overcome their intrinsic shortcomings and boost their efficiency via synergistic effects. This article provides an overview of recent efforts to utilize nanomaterials with superior properties to propose effective platforms for AD treatment. The underlying mechanismsthat are involved in modulating Aβ aggregation are discussed. The summary of nanomaterials-based modulation of Aβ aggregation may help researchers to understand the critical roles in therapeutic agents and provide new insight into the exploration of more promising anti-amyloid agents and tactics in AD theranostics.

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“…They have the characteristics of low toxicity, large speci c surface area, easy controllable surface assembly, and high speci city (Chatterjee et al 2021). Anand et al (Anand et al 2021) found that AuNPs surface-functionalized with a plant-based amino acid mimosine can attenuate Aβ brillization and neuronal toxicity. AuNPs were labeled to study AD and other neurodegenerative, neurovascular, and other neuropsychiatric diseases (Perets et al 2019).…”

Section: Introductionmentioning

confidence: 99%

Protective mechanism of gold nanoparticles on human neural stem cells injured by β-amyloid protein

Wang

Shen

Song

et al. 2022

Preprint

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BACKGROUND AND PURPOSE Alzheimer’s disease (AD) is a neurodegenerative disorder with progressive memory loss in dementia. Gold nanoparticles (AuNPs) were reported beneficial for human neural stem cells (hNSCs) treated with Amyloid-beta (Aβ), but the neuroprotective mechanisms still are unknown. METHODS Cell Counting Kit-8 (CCK-8) was performed to detect hNSCs viability. The content of interleukin 6 (IL-6) and tumor necrosis factor-alpha (TNF-α) was analyzed by enzyme-linked immunosorbent (ELISA) assay. Immunocytochemistry was carried out to determinate Tuj-1 and glial fibrillary acidic protein (GFAP). The reactive oxygen species (ROS) and JC-1 assay kits were performed to detect ROS generation and mitochondrial membrane potential. Quantitative PCR (qPCR) and Western blot assessments were also used to detect related gene expression intracellularly or in the supernatant. RESULTS The pro-inflammation IL-6 and TNF-α were significantly decreased in the AuNPs co-treatment group. AuNPs could ameliorate neural stem cell differentiation inhibition due to Aβ accumulation. AuNPs co-treatment repressed the high expression of total tau (T-tau), phosphorylated tau (P-tau), and Aβ protein caused by the Aβ treatment. The apoptosis rate of hNSCs induced by Aβ was inhibited by AuNPs co-treatment and the expression of proteins associated with apoptosis was also reduced in AuNPs co-treatment group. Aβ-induced decreased mitochondrial membrane potential and mitochondria in the hNSCs were damaged, while AuNPs co-treatment showed the protective effect on mitochondrial membrane potential. Co-treatment with AuNPs significantly increased dynamin-related protein 1 (DRP1), nuclear respiratory factor 1 (NRF1), and mitochondrial transcription factor A (TFAM) mRNA level. AuNPs may improve mitochondrial function impairment due to Aβ by elevating mitochondrial membrane potential, upregulating regulators of mitochondrial biogenesis, and inhibiting ROS production. hNSCs transfected with miR-21-5p inhibitor reversed AuNPs mediated cytoprotection induced by Aβ. miR-21-5p was involved in AuNPs protecting against Aβ-induced cell toxicity by reduced mitochondrial function. CONCLUSION AuNPs can protect hNSCs from Aβ injury by up-regulating miR-21-5p and protecting mitochondrial function.

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Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity

Cited by 24 publications

References 78 publications

Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology

Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology

Nanomaterials for Modulating the Aggregation of β-Amyloid Peptides

Protective mechanism of gold nanoparticles on human neural stem cells injured by β-amyloid protein

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