Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Shariatizi, Sajad; Meratan, Ali Akbar; Ghasemi, Ali; Nemat‐Gorgani, Mohsen

doi:10.1016/j.ijbiomac.2015.06.030

Cited by 61 publications

(36 citation statements)

References 81 publications

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“…Amyloid diseases predominantly involve the aggregation of specific proteins, such as the prion protein or the amyloid β-peptide, but fibrils can be formed by many other peptides and proteins [3]. Natural phenolic compounds, a long family of plant substances, are one of the most actively investigated categories of potential amyloid inhibitors [4][5][6]. More than 8,000 plant polyphenols are currently known and more than 4,000 flavonoids have been identified among them [7].…”

Section: Introductionmentioning

confidence: 99%

“…Polyphenols containing a higher number of aromatic rings, hydroxyl and keto groups and possess a high degree of planarity, have the largest inhibititory activity [18]. A structure-function relationship study suggested that the presence of at least two phenolic rings with two to six atomlong linkers, along with a minimum number of three hydroxyl groups on the aromatic rings, are essential for effi-cient inhibition exerted by polyphenols [5]. The mechanism of inhibition of amyloid formation is not identical for all natural polyphenols.…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Kotormán

Kasi

Halász

et al. 2017

PPL

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Abstract:The aim of the present study was to examine the potential role and applicability of dietary supplements in reducing the risk of development of amyloid diseases associated with the gastrointestinal tract, such as type II diabetes. Trypsin, a well-known serine protease was used as a model protein in our experiments. The effect of various red wines on the formation of amyloid-like fibrils of trypsin was studied in vitro, in aqueous ethanol, at pH 7.0. Turbidity measurements, aggregation kinetics experiments, Congo red binding assays and electronic circular dichroism spectroscopic measurements were used to follow the aggregation process in the presence or absence of various red wines. The results suggest that red wines effectively inhibit the formation of amyloid-like fibrils of trypsin and the inhibitory effect is dose-dependent. The extent of inhibition was found to be proportional to the total concentration of phenolic compounds.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Kotormán

Kasi

Halász

et al. 2017

PPL

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“…Recently, some authors have reported on inhibition of fibrillation as well as destabilization of preformed fibrils using polyphenols [13,14]. Polyethylene glycols (PEGs) are nontoxic, biocompatible, water-soluble, hydrophilic non-ionic polymers that can interact with proteins through hydrogenbonding or hydrophobic interactions [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Amyloid-like Fibril Formation by Trypsin in Aqueous Ethanol. Inhibition of Fibrillation by PEG

Kotormán

Simon

Borics

et al. 2015

PPL

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Abstract:The formation of amyloid-like fibrils was studied by using the well-known serine protease trypsin as a model protein in the presence of ethanol as organic solvent. Trypsin forms amyloid-like fibrils in aqueous ethanol at pH = 7.0. The dye Congo red (CR) was used to detect the presence of amyloid-like fibrils in the samples. The binding of CR to fibrils led to an increase in absorption intensity and a red shift in the absorption band of CR. Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) binding assays were employed to characterize amyloid-like fibril formation. The ThT binding assay revealed that the protein exhibited maximum aggregation in 60% (v/v) ethanol after incubation for 24 h at 24 o C. The ANS binding results indicated that the hydrophobic residues were more exposed to the solvent in the aggregated form of the protein. The effects of polyethylene glycol (PEG) on the formation of amyloid-like fibrils was studied in vitro. The aggregation of trypsin was followed via the kinetics of aggregation, the far-UV circular dichroism (CD) and transmission electron microscopy (TEM) in the presence and absence of PEG. The CD measurements indicated that the protein aggregates have a cross-beta structure in 60% ethanol. TEM revealed that trypsin forms fibrils with a thread-like structure. The inhibitory effect of PEG on the aggregation of trypsin increased with rising PEG concentration. PEG therefore inhibits the formation of amyloid-like fibrils of trypsin in aqueous ethanol.

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“…61,54,74 Even globular proteins not considered endogenously amyloidogenic have been investigated for their aggregation behavior under destabilizing conditions with the presence of NPs. 75–81 An example is BSA, a highly inert serum protein whose amyloid aggregation was observed after being exposed to polystyrene NPs or AuNPs. 36,82 Additional structural analysis indicates that the NPs could induce irreversible conformational changes in BSA.…”

Section: An Overview Of Np-mediated Protein Amyloid Aggregationmentioning

confidence: 99%

“…Though not natively amyloidogenic, lysozyme has been linked with hereditary systemic amyloidosis. 74,76,78–81,83 Small molecules such as polyphenols, cysteine, zinc ions and various dyes have been found to inhibit lysozyme aggregation, 78–81 while several metallic NPs have been shown to induce or promote lysozyme amyloids. 76,83 Zhang et al investigated the interaction between lysozyme and AuNPs, and found that AuNPs rendered protein aggregates.…”

Section: An Overview Of Np-mediated Protein Amyloid Aggregationmentioning

confidence: 99%

Modulating protein amyloid aggregation with nanomaterials

Wang

Pilkington

Sun

et al. 2017

Environ. Sci.: Nano

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Direct exposure or intake of nanopaticles (NPs) to the human body can invoke a series of biological responses, some of which are deleterious, and as such the role of NPs in vivo requires thorough examination. Over the past decade, it has been established that biomolecules such as proteins can bind NPs to form a ‘corona’, where the structures and dynamics of NP-associated proteins can assign new functionality, systemic distribution and toxicity. However, the behavior and fate of NPs in biological systems are still far from being fully understood. Growing evidence has shown that some natural or artificial NPs could either up- or down-regulate protein amyloid aggregation, which is associated with neurodegenerative diseases like Alzheimer’s and Parkinson’s diseases, as well as metabolic diseases such as type 2 diabetes. These effects can be either indirect (e.g., through a crowding effect) or direct, depending on the NP composition, size, shape and surface chemistry. However, efforts to design anti-amyloid NPs for biomedical applications have been largely hindered by insufficient understanding of the complex processes, even though proof-of-concept experiments have been conducted. Therefore, exploring the general mechanisms of NP-meditated protein aggregation marks an emerging field in bio-nano research and a new stage of handling nanotechnology that not only aids in elucidating the origin of nanotoxicity, but also provides a foundation for engineering de novo anti-amyloid nanomedicines. In this review, we summarize research on NP-mediated protein amyloid aggregation, with the goal of contributing to sustained nanotechnology and safe nanomedicine against amyloid diseases.

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Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Cited by 61 publications

References 81 publications

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Amyloid-like Fibril Formation by Trypsin in Aqueous Ethanol. Inhibition of Fibrillation by PEG

Modulating protein amyloid aggregation with nanomaterials

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