Photothermal ablation of amyloid aggregates by gold nanoparticles

Triulzi, Robert C.; Dai, Qinggang; Zou, Jianhua; Leblanc, Roger M.; Gu, Qun; Orbulescu, Jhony; Huo, Qun

doi:10.1016/j.colsurfb.2007.12.006

Cited by 61 publications

(51 citation statements)

References 33 publications

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“…Therefore, the cysteine used to coat the AuNPs must be capable of binding hydrophobic moieties of misfolding proteins, thereby preventing their aggregation and thus creating an environment for their refolding. It was observed previously that AuNPs are capable of reversing protein aggregation when combined with light energy (19). Based on the previous study and our current study, it appears that AuNPs may possess the capability to suppress aggregation of proteins, and may thus possibly facilitate their refolding.…”

Section: Figsupporting

confidence: 75%

“…Furthermore, the prospects of AuNPs serving as some form of artificial chaperone systems have broad implications in the biomedical and protein biotechnology sectors. For example, AuNPs have been proposed as potential therapies as exposure of protein aggregates to these nanoparticles with accompanying application of photothermal treatment led to the disaggregation of the protein complexes suggesting that AuNPs could be used to treat conditions such as Alzheimer's disease (19). In a previous study, it was observed that AuNPs improved the efficiency of amplifying DNA by the polymerase chain reaction (23).…”

Section: Figmentioning

confidence: 99%

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Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

et al. 2013

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Gold nanoparticles show a lot of promise as potential agents for drug delivery and disease diagnosis. Because of this, it is important that the interaction between gold nanoparticles and biomolecules be well characterized to avoid undesirable consequences. In this study, gold nanoparticles were synthesized by the reduction of gold salt by sodium borohydride in the presence of cysteine as the capping agent. The physical features of the nanoparticles were analyzed using Ultraviolet-Visible spectrophotometry and transmission electron microscopy. The interaction between gold nanoparticles and the following proteins: bovine serum albumin, citrate synthase, malate dehydrogenase, and human heat shock protein 70 was investigated by UV-Vis spectrophotometry. The stability of the proteins against heat stress was assessed by monitoring their aggregation at 48 8C, either in the presence or absence of gold nanoparticles. The gold nanoparticles were capable of suppressing the heat-induced aggregation of the proteins. Furthermore, apart from possessing independent protein-aggregation suppression function, the AuNPs also augmented the chaperone function of human heat shock protein 70. Findings from this study demonstrate that cyteinecoated gold nanoparticles exhibit chaperone-like activity and have the capability to stabilize proteins to which they may be conjugated. V C 2013 IUBMB Life, 65(5): 454-461, 2013.

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Section: Figsupporting

confidence: 75%

Section: Figmentioning

confidence: 99%

Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

et al. 2013

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“…Various drug nano-carriers have been successfully synthesized to transport small molecules, especially hydrophilic ones, across the BBB. [13][14][15][16][17] So, if NPs can inhibit the process of fibrillogenesis or disaggregate amyloid fibrils, 18 they offer great potential to be used as drugs to control neurodegenerative amyloid disease. On the other hand, detailed information about the interactions between NPs and amyloid proteins could shed light on the mechanism of fibril formation at the molecular level, an area which…”

Section: Introductionmentioning

confidence: 99%

Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor

Mohammadi¹,

Nikkhah²,

Hosseinkhani³

2017

IJN

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The aggregation of alpha-synuclein (αS), natively unstructured presynaptic protein, is a crucial factor leading to the pathogenesis of Parkinson’s disease (PD) and other related disorders. Recent studies have shown prefibrillar and oligomeric intermediates of αS as toxic to the cells. Herein, split-luciferase complementation assay is used to design a “signal-on” biosensor to monitor oligomerization of A53T αS inside the cells. Then, the effect of carbon-based nanomaterials, such as graphene quantum dots (GQDs) and graphene oxide quantum dots (GOQDs), on A53T αS oligomerization in vitro and in living cells is investigated. In this work, for the first time, it was found that GQDs at a concentration of 0.5 μg/mL can promote A53T αS aggregation by shortening the nucleation process, which is the key rate-determining step of fibrillation, thereby making a signal-on biosensor. While these nanomaterials may cross the blood–brain barrier because of their small sizes, the interaction between αS and GQDs may contribute to PD etiology.

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“…Moreover, feasibility in conjugating various drugs, peptides, proteins, antibodies, etc., made them suitable nanoparticulate drug delivery system in the field of oncology. Furthermore, apart from their control over the size, ease in preparation, the presence of carboxyl and amine groups help them in surface modification that could be efficiently targeted to attain site specificity (Gibson et al, 2007;Kattumuri et al, 2007;Triulzi et al, 2008;Fent et al, 2009;Lu et al, 2009). Active targeting drug delivery is the method for transporting chemotherapeutic agents to the diseased cells (Peer et al, 2007;Kamaly et al, 2012;Zhang et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Improved anti-tumor activity of oxaliplatin by encapsulating in anti-DR5 targeted gold nanoparticles

2016

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Oxaliplatin is one of the chemotherapeutic agents in the first line therapy for treatment of colorectal cancer. But, limitations of chemotherapy affects the clinical applicability of oxaliplatin depriving its activity at targeted site attributed to the lack of site specificity. This limitation paves the way for undesirable toxic effects to healthy cells resulting in sub-standard drug amount at the tumors obliging for increased dose. The present study emphasizes on formulating gold nanoparticles encapsulating oxaliplatin and later conjugating with anti-DR5 antibody for improved anti-cancer activity in a synergistic and site-specific manner. Oxaliplatin immuno-nanoparticles (Co-Ox-AuNPs) had shown sustained release and confirmed by fluorescence and flow cytometry studies. MTT assay exhibited 3-fold decrease in cell viability of nanoparticles comparable to oxaliplatin. Triple fluorescence method employed in HCT 116 and MCF-7 cells justified its site specificity. Annexin-propidium iodide (PI) and Acridine orangeethidium bromide assays further supported the apoptotic activity. Moreover, caspasedependent molecular mechanism behind oxaliplatin induced anti-cancer activity was explored by western blot analysis. Reduction in tumor size and volume in xenograft tumor models justified its in vitro activity. Oxaliplatin side effects were analyzed in mice and were confirmed for their clinical efficacy highlighting our formulation as an alternative to chemotherapy.

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Photothermal ablation of amyloid aggregates by gold nanoparticles

Cited by 61 publications

References 33 publications

Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

Investigation of the effects of carbon-based nanomaterials on A53T alpha-synuclein aggregation using a whole-cell recombinant biosensor

Improved anti-tumor activity of oxaliplatin by encapsulating in anti-DR5 targeted gold nanoparticles

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