Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme

Wang, Steven S.‐S.; Liu, Kuan-Nan; Lee, Wen-Hsuan

doi:10.1016/j.bpc.2009.06.010

Cited by 87 publications

(33 citation statements)

References 86 publications

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“…This superior inhibitory potency of pre-incubated curcumin was highly associated with curcumin dimeric species formed during the course of its preincubation. 74 Given the propensity for lysozyme to form high-quality crystals for X-ray structure determination, this system could serve as an excellent structural model for examining the mechanism of curcumin–protein interactions.…”

Section: Direct Molecular Targets Of Curcuminmentioning

confidence: 99%

Multitargeting by curcumin as revealed by molecular interaction studies

et al. 2011

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Curcumin (diferuloylmethane), the active ingredient in turmeric (Curcuma longa), is a highly pleiotropic molecule with anti-inflammatory, anti-oxidant, chemopreventive, chemosensitization, and radiosensitization activities. The pleiotropic activities attributed to curcumin come from its complex molecular structure and chemistry, as well as its ability to influence multiple signaling molecules. Curcumin has been shown to bind by multiple forces directly to numerous signaling molecules, such as inflammatory molecules, cell survival proteins, protein kinases, protein reductases, histone acetyltransferase, histone deacetylase, glyoxalase I, xanthine oxidase, proteasome, HIV1 integrase, HIV1 protease, sarco (endo) plasmic reticulum Ca2+ ATPase, DNA methyltransferases 1, FtsZ protofilaments, carrier proteins, and metal ions. Curcumin can also bind directly to DNA and RNA. Owing to its β-diketone moiety, curcumin undergoes keto–enol tautomerism that has been reported as a favorable state for direct binding. The functional groups on curcumin found suitable for interaction with other macromolecules include the α, β-unsaturated β-diketone moiety, carbonyl and enolic groups of the β-diketone moiety, methoxy and phenolic hydroxyl groups, and the phenyl rings. Various biophysical tools have been used to monitor direct interaction of curcumin with other proteins, including absorption, fluorescence, Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy, surface plasmon resonance, competitive ligand binding, Forster type fluorescence resonance energy transfer (FRET), radiolabeling, site-directed mutagenesis, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), immunoprecipitation, phage display biopanning, electron microscopy, 1-anilino-8-naphthalene-sulfonate (ANS) displacement, and co-localization. Molecular docking, the most commonly employed computational tool for calculating binding affinities and predicting binding sites, has also been used to further characterize curcumin’s binding sites. Furthermore, the ability of curcumin to bind directly to carrier proteins improves its solubility and bioavailability. In this review, we focus on how curcumin directly targets signaling molecules, as well as the different forces that bind the curcumin–protein complex and how this interaction affects the biological properties of proteins. We will also discuss various analogues of curcumin designed to bind selective targets with increased affinity.

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Section: Direct Molecular Targets Of Curcuminmentioning

confidence: 99%

Multitargeting by curcumin as revealed by molecular interaction studies

et al. 2011

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“…Cur activity towards Aβ42, hen egg-white lysozyme (HEWL) and human insulin amyloidogenic polypeptide (hIAPP) belongs to the first category of inhibitors: Cur inhibits Aβ42 peptide oligomerization, promoting the deposition of fibrils in vitro and in vivo [188,189], and counteracts HEWL aggregation, affecting also preformed fibrils, determining, in both cases, the formation of short, sheared fibrillar species [190]. While the fibrillar aggregates that are formed by Aβ and HEWL in the presence of Cur are devoid of cytotoxicity [182,191], this seems not to be the case for hIAPP: circular dichroism (CD) and nuclear magnetic resonance (NMR) analyses reveal that Cur inhibits the structural transition of hIAPP to the α-helical intermediate and slows down the aggregation kinetics, but it neither inhibits the deposition of short fibrils nor disaggregates β-sheet assemblies of hIAPP [192] and, while partially relieving exogenous hIAPP toxicity to INS cells, fails to protect against cytotoxicity in either INS cells overexpressing hIAPP or hIAPP transgenic rat islets [193].…”

Section: The Anti-amyloid Properties Of Natural Phenols and Polyphmentioning

confidence: 99%

Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

Stefani

Rigacci

2013

IJMS

192

127

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Amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity. Consequently, compounds counteracting amyloid aggregation have been investigated for their ability (i) to stabilize toxic amyloid precursors; (ii) to prevent the growth of toxic oligomers or speed that of fibrils; (iii) to inhibit fibril growth and deposition; (iv) to disassemble preformed fibrils; and (v) to favor amyloid clearance. Natural phenols, a wide panel of plant molecules, are one of the most actively investigated categories of potential amyloid inhibitors. They are considered responsible for the beneficial effects of several traditional diets being present in green tea, extra virgin olive oil, red wine, spices, berries and aromatic herbs. Accordingly, it has been proposed that some natural phenols could be exploited to prevent and to treat amyloid diseases, and recent studies have provided significant information on their ability to inhibit peptide/protein aggregation in various ways and to stimulate cell defenses, leading to identify shared or specific mechanisms. In the first part of this review, we will overview the significance and mechanisms of amyloid aggregation and aggregate toxicity; then, we will summarize the recent achievements on protection against amyloid diseases by many natural phenols.

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“…52 Analogous findings regarding the fibrilforming ability were observed in hen egg-white lysozyme, a food protein with high sequence homology to bovine α-LA. 9,53,54 It was generally accepted that fibrillation of the aforesaid food proteins are affected by the protein concentration, seeding, heating time, and shearing or stirring during heating. 13,55,56 Notably, ANS has been shown to interact with proteins by conformation-specific hydrophobic interactions and rather nonspecific electrostatic interactions.…”

Section: Discussionmentioning

confidence: 99%

Fibril Formation of Bovine α-Lactalbumin Is Inhibited by Glutathione

et al. 2011

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The current research is aimed at exploring the inhibitory effect of glutathione on fibril formation of an important four disulfide bond-containing whey protein, α-lactalbumin. Through numerous spectroscopic techniques and transmission electron microscopy, we found that the inhibition of amyloid formation of α-lactalbumin was dependent on the glutathione concentration and fibrillation was significantly attenuated in the presence of 5 mM glutathione. Moreover, the data from the measurements using 4,4′-dithiodipyridine reagent revealed that the treatment of α-lactalbumin with glutathione led to the exposure of sulfhydryl groups. Also, the observed inhibition of α-lactalbumin by glutathione was correlated with the reduction of disulfide bridges of protein. The results presented here suggest that the addition of food compatible reducing agent/dietary supplement such as glutathione would be useful for preventing the formation of milk protein fibrillar aggregates. The presence of these resulting aggregates can then, in turn, be used to modulate the key properties of food products such as protein beverage and yogurt.

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Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme

Cited by 87 publications

References 86 publications

Multitargeting by curcumin as revealed by molecular interaction studies

Multitargeting by curcumin as revealed by molecular interaction studies

Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

Fibril Formation of Bovine α-Lactalbumin Is Inhibited by Glutathione

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