Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin

Anand, Bibin G.; Dubey, Kriti; Shekhawat, Dolat Singh; Kar, Karunakar

doi:10.1021/acs.biochem.6b00418

Cited by 46 publications

(55 citation statements)

References 31 publications

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“…Larger metal nanoparticles elicited a stronger inhibitory effect on amyloidosis than smaller nanoparticles of similar surface functionalization . Silver nanoparticles (AgNPs) capped with citrate, chitosan, or natural products have also been reported to inhibit the aggregation of amyloid proteins …”

Section: Introductionmentioning

confidence: 99%

Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition

Huma

Javed

Zhang

et al. 2020

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Multidrug resistance of bacteria is a major challenge due to the wide‐spread use of antibiotics. While a range of strategies have been developed in recent years, suppression of bacterial activity and virulence via their network of extracellular amyloid has rarely been explored, especially with nanomaterials. Here, silver nanoparticles and nanoclusters (AgNPs and AgNCs) capped with cationic branched polyethylenimine polymer are synthesized, and their antimicrobial potentials are determined at concentrations safe to mammalian cells. Compared with the ultrasmall AgNCs, AgNPs entail stronger binding to suppress the fibrillization of FapC, a major protein constituent of the extracellular amyloid matrix of Pseudomonas aeruginosa. Both types of nanoparticles exhibit concentration‐dependent antibiofilm and antimicrobial properties against P. aeruginosa. At concentrations of 1 × 10−6 m or below, both the bactericidal activity of AgNCs and the antibiofilm capacity of AgNPs are associated with their structure‐mediated bio–nano interactions but not ion release. For AgNPs, specifically, their antibiofilm potency correlates with their capacity of FapC fibrillization inhibition, but not with their bactericidal activity. This study demonstrates the antimicrobial potential of safe nanotechnology through the novel route of amyloidosis inhibition.

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Section: Introductionmentioning

confidence: 99%

Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition

Huma

Javed

Zhang

et al. 2020

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“…[1,2] Until now, 35 different proteins, including amyloid-β (Aβ), α -synuclein, and huntingtin from lesions of AD, PD, and HD, respectively, have been found to form β-amyloid aggregates, which causes severe damage to neurons. [3,4] Despite the differences in their primary structures, all amyloid proteins share common mechanisms to form morphologically and immunologically similar aggregates, such as ring-shaped amyloid oligomers or amyloid fibrils. [5] The formation of amyloid fibrils is considered as a consequence of protein misfolding.…”

Section: Introductionmentioning

confidence: 99%

“…[11,12] In addition, nanometer-sized materials coated with specific molecules were also found to be capable of inhibiting the fibrillation process of proteins. [4,[13][14][15][16] To the best of our knowledge, very few articles have been reported concerning the synthetic polymers to inhibit the formation of amyloid fibrils. [17][18][19] Poly(lactic acid) (PLA) is a well-known synthetic polymer, widely used in biomedical applications because of its FDA approval for the clinical use.…”

Section: Introductionmentioning

confidence: 99%

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Gelatin grafted poly(D,L‐lactide) as an inhibitor of protein aggregation: An in vitro case study

Balavigneswaran

Kumar

Kumar³

et al. 2020

Biopolymers

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Amyloids are a group of proteins that are capable of forming aggregated amyloid fibrils, which is responsible for many neurodegenerative diseases including Alzheimer's disease (AD). In our previous study, synthesis and characterization of star‐shaped poly(D,L‐lactide)‐b‐gelatin (ss‐pLG) have been reported. In the present work, we have extended our work to study ss‐pLG against protein aggregation. To the best of our knowledge, this is the first report on the inhibition of amyloid fibrillation by protein grafted poly(D,L‐lactide). Bovine serum albumin (BSA) was chosen as the model protein, which readily forms fibril under high temperature. We found that ss‐pLG efficiently suppressed the fibril formation of BSA compared with gelatin (Gel), which was supported by Thioflavin T assay, circular dichroism (CD) spectroscopy and atomic force microscopy (AFM). In addition, ss‐pLG significantly curtailed amyloid‐induced hemolysis. We also found that incubation of ss‐pLG with neuroblastoma cells (MC65) protected the cells from fibril‐induced toxicity. The rescuing efficiency of ss‐pLG was better than Gel, which could be attributed to the reduced lamella thickness in branched ss‐pLG. These results suggest the significance of gelatin grafting, which probably allows gelatin to interact with the key residues of the amyloidogenic core of BSA effectively.

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“…In general, fluorophores used in biological applications -Thioflavin, Cyanine dyes etc. have strong emission within 400 nm to 750 nm wavelength range 23,24 . Longer excitation wavelength of 1064 nm is hence chosen to avoid the overwhelming fluorescence background from fluorophores.…”

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confidence: 99%

(Cu2O-Au) – Graphene - Au layered structures as efficient near Infra - Red SERS substrates

Nair

Murukeshan

2020

Sci Rep

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Near Infra-Red Surface Enhanced Raman Spectroscopy (NIR SERS) has gained huge attention in recent years as the conventional visible SERS suffers from overwhelming fluorescence background from the fluorophore resulting in the masking of Raman signals. In this paper, we propose a novel multilayered SeRS substrate-(cu 2 O-Au)-Graphene-Au-for efficient NIR SERS applications. The proposed structure has a monolayer of Cu 2 O-Au core-shell particles on a Au substrate with 1 nm thick graphene spacer layer. Mie simulations are used to optimize the aspect ratios of core-shell particles to shift their plasmon resonances to NIR region using MieLab software. Further, Finite Difference Time Domain (FDTD) simulations using Lumerical software are used for the design of the multiparticle layered SERS substrate as MieLab software works only for single particle systems. Designed structure is shown to provide high field enhancement factor of the order of 10 8 at an excitation of 1064 nm thus ensuring the possibility of using the proposed structure as efficient NIR SERS substrate which could probably be used for various NIR sensing applications.

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Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin

Cited by 46 publications

References 31 publications

Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition

Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition

Gelatin grafted poly(D,L‐lactide) as an inhibitor of protein aggregation: An in vitro case study

(Cu2O-Au) – Graphene - Au layered structures as efficient near Infra - Red SERS substrates

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