Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR)

Bae, Song Yi; Kim, Seulgi; Hwang, Heejin; Kim, Hyun-Kyung; Kim, Jae Ho; Lee, Sang Yoon; Kim, T. Doohun

doi:10.1016/j.bbrc.2010.08.088

Cited by 35 publications

(18 citation statements)

References 29 publications

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“…It has been observed that various polyphenols could cause dissociation of amyloid fibrils [26,27]. This polyphenol-induced dissociation of the amyloid fibrils occurs because these polyphenols disrupt the sheet-sheet interaction of amyloid fibrils either directly or indirectly.…”

Section: Amyloid Formation Of Li22mentioning

confidence: 98%

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262

Kim¹,

Bae²,

Kim³

et al. 2012

International Journal of Biological Macromolecules

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Section: Amyloid Formation Of Li22mentioning

confidence: 98%

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262

Kim¹,

Bae²,

Kim³

et al. 2012

International Journal of Biological Macromolecules

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“…The array of natural phenols being tested as potential inhibitors of amyloid aggregation becomes wider and wider every day and now includes also tannic acid [207,313] and the product of tannin hydrolysis ellagic acid [314]; several flavones, like apigenin [315,316], baicalein [315,317,318], kaempferol [260,261,263,264,271,319], morin [265,320,321], fisetin [259,260,321], rutin (the glycoside of quercetin with the disaccharide rutinose) [322,323] and luteolin [260,324]; rottlerin, already known as a PKC-δ inhibitor [325,326]; the anthocyanidin malvidin, the main responsible for the red color of wine [327]; the stilbenes piceatannol [328] and the resveratrol-derived dimer ɛ-viniferin glucoside [329]; and, finally, ferulic acid (related to trans-cinnamic acid) [189,263,264,330–332]. …”

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

189

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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“…The general mechanism of EGCG has now been confirmed in various misfolded protein systems [81,95,96] and the yeast prion Sup35 [86]. However, mechanistic details seem to depend on the stability of the protein aggregates that are formed with the aid of EGCG.…”

Section: Mechanism Of Egcg Interventionmentioning

confidence: 97%

“…Since then, it has been shown that EGCG binds directly to a large number of proteins that are involved in protein misfolding diseases and that EGCG inhibits their fibrillization. Examples include αS [81,82], Aβ [36,82], transthyretin [83], lysozyme [84], the prion protein PrP [85], and the yeast prion Sup35 [86].…”

Section: Mechanism Of Egcg Interventionmentioning

confidence: 99%

Natural Compounds May Open New Routes to Treatment of Amyloid Diseases

Bieschke

2013

Neurotherapeutics

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Protein misfolding disorders, such as Alzheimer's disease and Parkinson's disease, have in common that a protein accumulates in an insoluble form in the affected tissue. The process of aggregation follows a mechanism of seeded polymerization. Although the toxic species is still not well defined, the process, rather than the end product, of fibril formation is likely the main culprit in amyloid toxicity. These findings suggest that therapeutic strategies directed against the protein misfolding cascade should focus on depleting aggregation intermediates rather than on large fibrillar aggregates. Recent studies involving natural compounds have suggested new intervention strategies. The polyphenol epi-gallocatechine-3-gallate (EGCG), the main polyphenol in Camilla sinensis, binds directly to a large number of proteins that are involved in protein misfolding diseases and inhibits their fibrillization. Instead, it promotes the formation of stable, spherical aggregates. These spherical aggregates are not cytotoxic, have a lower β-sheet content than fibrils, and do not catalyze fibril formation. Correspondingly, epi-gallocatechine-3-gallate remodels amyloid fibrils into aggregates with the same properties. Derivatives of Orcein, which is a phenoxazine dye that can be isolated from the lichen Roccella tinctoria, form a second promising class of natural compounds. They accelerate fibril formation of the Alzheimer's disease-related amyloid-beta peptide. At the same time these compounds deplete oligomeric and protofibrillar forms of the peptide. These compounds may serve as proof-of-principle for the strategies of promoting and redirecting fibril formation. Both may emerge as two promising new therapeutic approaches to intervening into protein misfolding processes.

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Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR)

Cited by 35 publications

References 29 publications

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262

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

Natural Compounds May Open New Routes to Treatment of Amyloid Diseases

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