keyword
https://read.qxmd.com/read/38338914/the-inhibition-effect-of-epigallocatechin-3-gallate-on-the-co-aggregation-of-amyloid-%C3%AE-and-human-islet-amyloid-polypeptide-revealed-by-replica-exchange-molecular-dynamics-simulations
#1
JOURNAL ARTICLE
Xuhua Li, Yu Zhang, Zhiwei Yang, Shengli Zhang, Lei Zhang
Alzheimer's disease and Type 2 diabetes are two epidemiologically linked diseases which are closely associated with the misfolding and aggregation of amyloid proteins amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP), respectively. The co-aggregation of the two amyloid proteins is regarded as the fundamental molecular mechanism underlying their pathological association. The green tea extract epigallocatechin-3-gallate (EGCG) has been extensively demonstrated to inhibit the amyloid aggregation of Aβ and hIAPP proteins...
January 29, 2024: International Journal of Molecular Sciences
https://read.qxmd.com/read/37762449/egcg-mediated-protection-of-transthyretin-amyloidosis-by-stabilizing-transthyretin-tetramers-and-disrupting-transthyretin-aggregates
#2
JOURNAL ARTICLE
Huizhen Zou, Shuangyan Zhou
Transthyretin amyloidosis (ATTR) is a progressive and systemic disease caused by the misfolding and amyloid aggregation of transthyretin (TTR). Stabilizing the TTR tetramers and disrupting the formed TTR aggregation are treated as a promising strategy for the treatment of ATTR. Previous studies have reported that epigallocatechin gallate (EGCG) can participate in the whole process of TTR aggregation to prevent ATTR. However, the interaction mechanism of EGCG in this process is still obscure. In this work, we performed molecular dynamics simulations to investigate the interactions between EGCG and TTR tetramers, and between EGCG and TTR aggregates formed by the V30M mutation...
September 15, 2023: International Journal of Molecular Sciences
https://read.qxmd.com/read/36829983/3d-printed-liquid-filled-capsules-of-concentrated-and-stabilized-polyphenol-epigallocatechin-gallate-developed-in-a-clinical-trial
#3
JOURNAL ARTICLE
Philippe-Henri Secretan, Victoire Vieillard, Olivier Thirion, Maxime Annereau, Hassane Sadou Yayé, Alain Astier, Muriel Paul, Thibaud Damy, Bernard Do
In vitro studies have shown that epigallocatechin gallate (EGCG), the most potent antioxidant of the green tea polyphenol catechins, is able to effectively prevent the formation of amyloid plaques and induce their clearance. However, its high chemical reactivity promotes high chemical instability, which represents a major obstacle for the development of pharmaceutical forms containing solubilized EGCG, an essential condition for a better systemic passage via the oral route. After discovering that EGCG forms a deep eutectic with choline chloride, we exploited this property to formulate and patent liquid-filled capsules containing 200-800 mg of soluble EGCG in easy-to-administer sizes...
February 9, 2023: Antioxidants (Basel, Switzerland)
https://read.qxmd.com/read/36724494/zinc-epigallocatechin-3-gallate-network-coated-nanocomposites-against-the-pathogenesis-of-amyloid-beta
#4
JOURNAL ARTICLE
Nicholas Andrikopoulos, Yuhuan Li, Aparna Nandakumar, John F Quinn, Thomas P Davis, Feng Ding, Nabanita Saikia, Pu Chun Ke
The aggregation of amyloid beta (Aβ) is a hallmark of Alzheimer's disease (AD), a major cause of dementia and an unmet challenge in modern medicine. In this study, we constructed a biocompatible metal-phenolic network (MPN) comprising a polyphenol epigallocatechin gallate (EGCG) scaffold coordinated by physiological Zn(II). Upon adsorption onto gold nanoparticles, the MPN@AuNP nanoconstruct elicited a remarkable potency against the amyloid aggregation and toxicity of Aβ in vitro. The superior performance of MPN@AuNP over EGCG@AuNP was attributed to the porosity and hence larger surface area of the MPN in comparison with that of EGCG alone...
February 1, 2023: ACS Applied Materials & Interfaces
https://read.qxmd.com/read/34688163/molecular-simulation-probes-the-potency-of-resveratrol-in-regulating-the-toxic-aggregation-of-mutant-v30m-ttr-fibrils-in-transthyretin-mediated-amyloidosis
#5
JOURNAL ARTICLE
G Chandrasekhar, E Srinivasan, P Chandra Sekar, S Venkataramanan, R Rajasekaran
Transthyretin (TTR) mediated amyloidosis is a highly ruinous illness that affects various organs by aggravating the deposition of misfolded or mutated TTR protein aggregates in tissues. Hence, hindering the formation of TTR amyloid aggregates could be a key strategy in finding an effective cure towards the aggravating disorder. In this analysis, we examined the subversive nature of point mutation, V30M, in TTR that promotes amyloidogenicity using discrete molecular dynamics (DMD) simulations. Besides, we probed the association of naturally occurring polyphenols: EGCG (a proven anti TTR aggregation agent as positive control), resveratrol and curcumin in mitigating the pathogenic repercussions of mutant TTR...
January 2022: Journal of Molecular Graphics & Modelling
https://read.qxmd.com/read/34594185/green-tea-polyphenol-epigallocatechin-gallate-in-amyloid-aggregation-and-neurodegenerative-diseases
#6
REVIEW
Luiza Fernandes, Thyago R Cardim-Pires, Debora Foguel, Fernando L Palhano
The accumulation of protein aggregates in human tissues is a hallmark of more than 40 diseases called amyloidoses. In seven of these disorders, the aggregation is associated with neurodegenerative processes in the central nervous system such as Alzheimer's disease (AD), Parkinson's disease (PD), and Huntington's disease (HD). The aggregation occurs when certain soluble proteins lose their physiological function and become toxic amyloid species. The amyloid assembly consists of protein filament interactions, which can form fibrillar structures rich in β-sheets...
2021: Frontiers in Neuroscience
https://read.qxmd.com/read/34208058/barriers-to-small-molecule-drug-discovery-for-systemic-amyloidosis
#7
JOURNAL ARTICLE
Gareth J Morgan
Inhibition of amyloid fibril formation could benefit patients with systemic amyloidosis. In this group of diseases, deposition of amyloid fibrils derived from normally soluble proteins leads to progressive tissue damage and organ failure. Amyloid formation is a complex process, where several individual steps could be targeted. Several small molecules have been proposed as inhibitors of amyloid formation. However, the exact mechanism of action for a molecule is often not known, which impedes medicinal chemistry efforts to develop more potent molecules...
June 11, 2021: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://read.qxmd.com/read/34013116/glomerulopathic-light-chain-mesangial-cell-interactions-sortilin-related-receptor-sorl1-and-signaling
#8
JOURNAL ARTICLE
Guillermo A Herrera, Luis Del Pozo-Yauner, Jiamin Teng, Chun Zeng, Xinggui Shen, Takahito Moriyama, Veronica Ramirez Alcantara, Bing Liu, Elba A Turbat-Herrera
INTRODUCTION: Deciphering the intricacies of the interactions of glomerulopathic Ig light chains with mesangial cells is key to delineate signaling events responsible for the mesangial pathologic alterations that ensue. METHODS: Human mesangial cells, caveolin 1 (CAV1), wild type (WT) ,and knockout (KO), were incubated with glomerulopathic light chains purified from the urine of patients with light chain-associated (AL) amyloidosis or light chain deposition disease...
May 2021: KI Reports
https://read.qxmd.com/read/33598831/aggregation-of-gelsolin-wild-type-and-g167k-r-n184k-and-d187n-y-mutant-peptides-and-inhibition
#9
JOURNAL ARTICLE
Mohanad Ahmad, Josephine Esposto, Camilla Golec, Colin Wu, Sanela Martic-Milne
Gelsolin, an actin-binding protein, is localized intra- and extracellularly in the bloodstream and throughout the body. Gelsolin amyloidosis is a disease characterized by several point mutations that lead to cleavage and fibrillization of gelsolin. The D187 mutation to N or Y leads to aggregation of peptide fragments with shortest aggregating peptide identified as 182SFNNGDCFILD192. Recently, G167 has also been identified as relevant gelsolin mutation, which leads to gelsolin deposits in kidneys, but its aggregation is much less understood...
June 2021: Molecular and Cellular Biochemistry
https://read.qxmd.com/read/33331220/two-polyphenols-with-diverse-mechanisms-towards-amyloidosis-differential-modulation-of-the-fibrillation-pathway-of-human-lysozyme-by-curcumin-and-egcg
#10
JOURNAL ARTICLE
Fatima Kamal Zaidi, Rajiv Bhat
The effect of two widely used polyphenols, curcumin and EGCG was investigated on the amyloid fibrillogenesis of the well-characterized model protein human lysozyme (HuL), associated with non-neuropathic systemic amyloidosis, towards exploring their efficacy as modulators of HuL amyloid aggregation and toxicity and unravelling their mechanism of action. Curcumin exerts its inhibitory influence towards HuL fibrillation by interacting with the prefibrillar and fibrillar intermediates resulting in complete suppression of fibrillation at ∼200 µM and effectively disaggregates preformed fibrils of HuL...
July 2022: Journal of Biomolecular Structure & Dynamics
https://read.qxmd.com/read/32169448/drug-based-magnetic-imprinted-nanoparticles-enhanced-lysozyme-amyloid-fibrils-cleansing-and-anti-amyloid-fibrils-toxicity
#11
JOURNAL ARTICLE
Chaoren Yan, Nan Zhang, Ping Guan, Peng Chen, Shichao Ding, Tongtong Hou, Xiaoling Hu, Jian Wang, Chaoli Wang
Lysozyme amyloid fibrils, the misfolding structures generated from natural state of lysozyme, are found to be related with non-neuropathic systemic amyloidosis. Therefore, inhibiting the formation of amyloid and disaggregating amyloid fibers are both effective strategies. Herein, we present a combination of Epigallocatechin-3-gallate (EGCG), imprinting technology and magnetic nanoparticles to obtain a kind of promising nanomaterials (MINs@EGCG) for amyloid inhibition, drug carrier and facile separation triple functions...
June 15, 2020: International Journal of Biological Macromolecules
https://read.qxmd.com/read/30739503/cell-assay-for-the-identification-of-amyloid-inhibitors-in-systemic-aa-amyloidosis
#12
JOURNAL ARTICLE
Ioana Puscalau-Girtu, Judith S Scheller, Stephanie Claus, Marcus Fändrich
Systemic AA amyloidosis is still, up to this day, a life-threatening complication of chronic inflammatory diseases. Despite the success of anti-inflammatory treatment, the prognosis of some AA patients is still poor, which is why therapies directed at the amyloidogenic pathway in AA amyloidosis are being sought after. The cell culture model of amyloid formation from serum amyloid A1 (SAA1) protein remodels crucial features of AA amyloid deposit formation in vivo. We here demonstrate how the cell model can be utilized for the identification of compounds with amyloid inhibitory activity...
March 2019: Amyloid: the International Journal of Experimental and Clinical Investigation
https://read.qxmd.com/read/30563837/combined-treatment-with-the-phenolics-epigallocatechin-3-gallate-and-ferulic-acid-improves-cognition-and-reduces-alzheimer-like-pathology-in-mice
#13
JOURNAL ARTICLE
Takashi Mori, Naoki Koyama, Jun Tan, Tatsuya Segawa, Masahiro Maeda, Terrence Town
"Nutraceuticals" are well-tolerated natural dietary compounds with drug-like properties that make them attractive as Alzheimer's disease (AD) therapeutics. Combination therapy for AD has garnered attention following a recent National Institute on Aging mandate, but this approach has not yet been fully validated. In this report, we combined the two most promising nutraceuticals with complementary anti-amyloidogenic properties: the plant-derived phenolics (-)-epigallocatechin-3-gallate (EGCG, an α-secretase activator) and ferulic acid (FA, a β-secretase modulator)...
February 22, 2019: Journal of Biological Chemistry
https://read.qxmd.com/read/30251653/inhibition-of-amyloid-fibril-formation-in-the-variable-domain-of-%C3%AE-6-light-chain-mutant-wil-caused-by-the-interaction-between-its-unfolded-state-and-epigallocatechin-3-o-gallate
#14
JOURNAL ARTICLE
Yoshito Abe, Naoki Odawara, Nantanat Aeimhirunkailas, Hinako Shibata, Naoki Fujisaki, Hirofumi Tachibana, Tadashi Ueda
BACKGROUND: Light chains are abnormally overexpressed from disordered monoclonal B-cells and form amyloid fibrils, which are then deposited on the affected organ, leading to a form of systemic amyloidosis known as AL (Amyloid Light chain) amyloidosis. A green tea catechin, epigallocatechin-3-O-gallate (EGCG), which is thought to inhibit various amyloidoses, is a potent inhibitor of amyloid fibril formation in AL amyloidosis. METHODS: An amyloidogenic variable domain in λ6 light chain mutant, Wil was incubated in the presence of EGCG...
December 2018: Biochimica et Biophysica Acta. General Subjects
https://read.qxmd.com/read/29882023/epigallocatechin-3-gallate-tolerability-and-impact-on-survival-in-a-cohort-of-patients-with-transthyretin-related-cardiac-amyloidosis-a-single-center-retrospective-study
#15
JOURNAL ARTICLE
Francesco Cappelli, Raffaele Martone, Giulia Taborchi, Sofia Morini, Simone Bartolini, Paola Angelotti, Silvia Farsetti, Carlo Di Mario, Federico Perfetto
Transthyretin-related (ATTR) cardiac amyloidosis is currently lacking a disease-modifying therapy. Despite demonstration of effectiveness in halting amyloid deposition, no study focused on epigallocatechin-3-gallate (EGCG) impact on patient survival. We sought to explore prognostic impact of EGCG in a cohort of lone cardiac ATTR patients. From the Florence Tuscan Regional Amyloid Centre database, we retrospectively selected ATTR patients treated with EGCG (675mg daily dose) for a minimum of 9 months, between March 2013 and December 2016...
September 2018: Internal and Emergency Medicine
https://read.qxmd.com/read/29843451/in-vitro-and-in-silico-studies-of-the-molecular-interactions-of-epigallocatechin-3-o-gallate-egcg-with-proteins-that-explain-the-health-benefits-of-green-tea
#16
REVIEW
Koichi Saeki, Sumio Hayakawa, Shogo Nakano, Sohei Ito, Yumiko Oishi, Yasuo Suzuki, Mamoru Isemura
Green tea has been shown to have beneficial effects on many diseases such as cancer, obesity, inflammatory diseases, and neurodegenerative disorders. The major green tea component, epigallocatechin-3- O -gallate (EGCG), has been demonstrated to contribute to these effects through its anti-oxidative and pro-oxidative properties. Furthermore, several lines of evidence have indicated that the binding affinity of EGCG to specific proteins may explain its mechanism of action. This review article aims to reveal how EGCG-protein interactions can explain the mechanism by which green tea/EGCG can exhibit health beneficial effects...
May 28, 2018: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://read.qxmd.com/read/29770336/epigallocatechin-3-gallate-reduces-neuronal-apoptosis-in-rats-after-middle-cerebral-artery-occlusion-injury-via-pi3k-akt-enos-signaling-pathway
#17
JOURNAL ARTICLE
Wang Nan, Xu Zhonghang, Chen Keyan, Liu Tongtong, Guo Wanshu, Xu Zhongxin
BACKGROUND/AIMS: Epigallocatechin-3-gallate (EGCG) has neuroprotective effects and the ability to resist amyloidosis. This study observed the protective effect of EGCG against neuronal injury in rat models of middle cerebral artery occlusion (MCAO) and investigated the mechanism of action of PI3K/AKT/eNOS signaling pathway. METHODS: Rat models of permanent MCAO were established using the suture method. Rat behavior was measured using neurological deficit score. Pathology and apoptosis were measured using HE staining and TUNEL...
2018: BioMed Research International
https://read.qxmd.com/read/28128355/epigallocatechin-3-gallate-preferentially-induces-aggregation-of-amyloidogenic-immunoglobulin-light-chains
#18
JOURNAL ARTICLE
Manuel Hora, Martin Carballo-Pacheco, Benedikt Weber, Vanessa K Morris, Antje Wittkopf, Johannes Buchner, Birgit Strodel, Bernd Reif
Antibody light chain amyloidosis is a rare disease caused by fibril formation of secreted immunoglobulin light chains (LCs). The huge variety of antibody sequences puts a serious challenge to drug discovery. The green tea polyphenol epigallocatechin-3-gallate (EGCG) is known to interfere with fibril formation in general. Here we present solution- and solid-state NMR studies as well as MD simulations to characterise the interaction of EGCG with LC variable domains. We identified two distinct EGCG binding sites, both of which include a proline as an important recognition element...
January 27, 2017: Scientific Reports
https://read.qxmd.com/read/28031465/aggregation-of-full-length-immunoglobulin-light-chains-from-systemic-light-chain-amyloidosis-al-patients-is-remodeled-by-epigallocatechin-3-gallate
#19
JOURNAL ARTICLE
Kathrin Andrich, Ute Hegenbart, Christoph Kimmich, Niraja Kedia, H Robert Bergen, Stefan Schönland, Erich Wanker, Jan Bieschke
Intervention into amyloid deposition with anti-amyloid agents like the polyphenol epigallocatechin-3-gallate (EGCG) is emerging as an experimental secondary treatment strategy in systemic light chain amyloidosis (AL). In both AL and multiple myeloma (MM), soluble immunoglobulin light chains (LC) are produced by clonal plasma cells, but only in AL do they form amyloid deposits in vivo We investigated the amyloid formation of patient-derived LC and their susceptibility to EGCG in vitro to probe commonalities and systematic differences in their assembly mechanisms...
February 10, 2017: Journal of Biological Chemistry
https://read.qxmd.com/read/27815860/phase-2-trial-of-daily-oral-epigallocatechin-gallate-in-patients-with-light-chain-amyloidosis
#20
RANDOMIZED CONTROLLED TRIAL
Sohsuke Meshitsuka, Sumito Shingaki, Masatoshi Hotta, Miku Goto, Makoto Kobayashi, Yuuichi Ukawa, Yuko M Sagesaka, Yasuyo Wada, Masanori Nojima, Kenshi Suzuki
Previous studies have suggested that an increase in mitochondrial reactive oxygen species may cause organ damage in patients with light-chain (AL) amyloidosis; however, this damage can be decreased by antioxidant-agent treatment. Epigallocatechin gallate (EGCG), the major natural catechin in green tea, has potent antioxidant activity. Because EGCG has recently been reported to have a favorable toxicity profile for treating amyloidosis, we sought to examine the clinical efficacy and toxicity of EGCG in patients with AL amyloidosis...
March 2017: International Journal of Hematology
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