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Littérature scientifique sur le sujet « Anti-amyloidogenic compounds »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 10 mars 2023

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Articles de revues sur le sujet "Anti-amyloidogenic compounds"

Porzoor, Afsaneh, Benjamin Alford, Helmut Hügel, Danilla Grando, Joanne Caine, and Ian Macreadie. "Anti-Amyloidogenic Properties of Some Phenolic Compounds." Biomolecules 5, no. 2 (2015): 505–27. http://dx.doi.org/10.3390/biom5020505.

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Hirohata, Mie, Kenjiro Ono, and Masahito Yamada. "Non-Steroidal Anti-Inflammatory Drugs as Anti-Amyloidogenic Compounds." Current Pharmaceutical Design 14, no. 30 (2008): 3280–94. http://dx.doi.org/10.2174/138161208786404173.

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Ziaunys, Mantas, and Vytautas Smirnovas. "Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties." Antioxidants 11, no. 10 (2022): 1887. http://dx.doi.org/10.3390/antiox11101887.

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Amyloidogenic protein/peptide aggregation into fibrillar aggregates is associated with multiple amyloidoses, including widespread neurodegenerative disorders. Despite years of research and a well-understood mechanism, there are still very few treatments available for the increasing number of amyloid-related disorders. In recent years, the search for potential anti-aggregation compounds has shifted toward naturally occurring molecules, with one of the most promising being epigallocatechin-3-gallate (EGCG). This polyphenolic compound was shown to inhibit the aggregation of several amyloidogenic proteins/peptides, including amyloid-beta (related to Alzheimer’s disease) and alpha-synuclein (related to Parkinson’s disease). However, multiple reports have indicated its limited stability under physiological conditions and the possibility of EGCG autoxidation products being the actual inhibitory compounds. In this work, we explore how different EGCG autoxidation products associate with non-aggregated insulin, as well as how they affect its aggregation and resulting fibril structure. We also show that there is a specific incubation time required for the emergence of compounds, which alters the amyloid aggregation process.

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Skibiszewska and Jankowska. "Can Short Peptides Be Inhibitors of Serum Amyloid a Protein Aggregation?" Proceedings 22, no. 1 (2019): 38. http://dx.doi.org/10.3390/proceedings2019022038.

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Tan, Mario A., Mark Wilson D. Lagamayo, Grecebio Jonathan D. Alejandro, and Seong Soo A. An. "Anti-Amyloidogenic and Cyclooxygenase Inhibitory Activity of Guettarda speciosa." Molecules 24, no. 22 (2019): 4112. http://dx.doi.org/10.3390/molecules24224112.

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Guettarda speciosa is known in traditional folk medicine for treating cough, cold, sore throat, fever, wounds, epilepsy, and headaches. To discover the scientific pharmacological potential of G. speciosa, we explore its anti-inflammatory, cytotoxicity, and inhibition of amyloid-beta (Aβ) aggregation effects. Cyclooxygenase assay of the G. speciosa CHCl3 (GSC) extract and G. speciosa MeOH (GSM) extract are more selective to COX-1 inhibition with a 50% inhibitory concentration (IC50) of 3.56 μg/mL for the GSC extract and 4.98 μg/mL for the GSM extract. Neuroblastoma SH-SY5Y inhibition and thioflavin T assay amyloid-beta (Aβ) aggregate inhibition of the GSM and GSC extracts showed their potential therapeutic effects against Alzheimer’s disease. The putative compounds from the LC-MS analysis could be responsible for the observed activities. The results suggest that G. speciosa possesses anti-inflammatory and anti-neurodegenerative properties and a promising lead as a source of pharmacologically active compounds.

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Yeo, Ji-Yun, Seul Lee, Min Sung Ko, et al. "Anti-Amyloidogenic Effects of Metasequoia glyptostroboides Fruits and Its Active Constituents." Molecules 28, no. 3 (2023): 1017. http://dx.doi.org/10.3390/molecules28031017.

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Alzheimer’s disease (AD) is a serious neurodegenerative brain disease that interferes with daily life. The accumulation of beta-amyloid (Aβ), along with oxidative stress-inducing neurocellular apoptosis, has been considered one of the causes of AD. Thus, the purpose of this study is to find natural products that can reduce Aβ accumulation. The ethanol extract of Metasequoia glyptostroboides Hu & Cheng fruits (Cupressaceae) significantly reduced the aggregation of Aβ into oligomers and fibrils determined by Thioflavin T (ThT) assay. The solvent-partitioned ethyl acetate layer was further separated based on the bioassay-guided isolation method combined with the ThT assay. As a result, five compounds were isolated and elucidated as taxoquinone (1), sugiol (2), suginal (3), sandaracopimarinol (4), and sandaracopimaradien-19-ol (5) by comparing NMR data with references. All the compounds significantly reduced the aggregation of Aβ and enhanced the disaggregation of pre-formed Aβ aggregates in a dose-dependent manner. Furthermore, the inhibition of Aβ aggregation by the compounds protected PC12 cells from Aβ aggregate-induced toxicity. Among the five compounds, sandaracopimarinol (4) and sandaracopimaradien-19-ol (5) were the most effective. These results suggest that M. glyptostroboides and isolated five compounds have a potential for further study to be developed as anti-AD agents.

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Quiroz, Jose Paredes, Andi Zeng, Michelle Young, et al. "Homotaurine and Curcumin Analogues as Potential Anti-Amyloidogenic Agents." Chemistry 5, no. 1 (2023): 223–41. http://dx.doi.org/10.3390/chemistry5010018.

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Currently, there is neither a cure for Alzheimer’s disease (AD) nor a way to stop the progressive death of neuronal cells associated with this devastating aliment. To date, there are only medications that temporarily slow its progression, and do not interfere with its pathogenesis. One of the hallmarks of AD is the presence of amyloid-beta plaques derived from the metabolism of the amyloid precursor protein, via the cleavage by beta followed by gamma secretase. Homotaurine, a naturally occurring small molecule found in some seaweeds, and curcumin, a phenolic antioxidant found in Curcuma longa, have been extensively studied as potential compounds to prevent/reverse plaque formation. In this study, libraries of chalcones and extended chalcones based on curcumin, as well as aminopropylsulfonamides inspired by homotaurine, were synthesized. Using fluorescence spectroscopic analysis with Thioflavin T, the anti-aggregation effect on Aβ42 was determined. A select number of newly synthesized chalcones and extended chalcone analogs were revealed to be potential anti-amyloidogenic agents. These were further evaluated with regard to their neurotoxicity/neuroprotection. The extended chalcone analogs that displayed the most anti-aggregation effect on Aβ42 were further analyzed in an MTT assay. Although none of the compounds alone displayed any neurotoxicity, none were able to provide neuroprotection against Aβ42.

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Marvastizadeh, Narges, Bahareh Dabirmanesh, Reza H. Sajedi та Khosro Khajeh. "Anti-amyloidogenic effect of artemin on α-synuclein". Biological Chemistry 401, № 10 (2020): 1143–51. http://dx.doi.org/10.1515/hsz-2019-0446.

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Abstractα-Synuclein fibrillation is now regarded as a major pathogenic process in Parkinson’s disease and its proteinaceous deposits are also detected in other neurological disorders including Alzheimer's disease. Therefore anti-amyloidegenic compounds may delay or prevent the progression of synucleinopathies disease. Molecular chaperones are group of proteins which mediate correct folding of proteins by preventing unsuitable interactions which may lead to aggregation. The objective of this study was to investigate the anti-amyloidogenic effect of molecular chaperone artemin on α-synuclein. As the concentration of artemin was increased up to 4 μg/ml, a decrease in fibril formation of α-synuclein was observed using thioflavin T (ThT) fluorescence and congo red (CR) assay. Transmission electron microscopy (TEM) images also demonstrated a reduction in fibrils in the presence of artemin. The secondary structure of α-synuclein was similar to its native form prior to fibrillation when incubated with artemin. A cell-based assay has shown that artemin inhibits α-synuclein aggregation and reduce cytotoxicity, apoptosis and reactive oxygen species (ROS) production. Our results revealed that artemin has efficient chaperon activity for preventing α-synuclein fibril formation and toxicity.

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Jiaranaikulwanitch, Jutamas, Hataichanok Pandith, Sarin Tadtong, et al. "Novel Multifunctional Ascorbic Triazole Derivatives for Amyloidogenic Pathway Inhibition, Anti-Inflammation, and Neuroprotection." Molecules 26, no. 6 (2021): 1562. http://dx.doi.org/10.3390/molecules26061562.

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Alzheimer’s disease (AD) is a common neurodegenerative disorder. The number of patients with AD is projected to reach 152 million by 2050. Donepezil, rivastigmine, galantamine, and memantine are the only four drugs currently approved by the United States Food and Drug Administration for AD treatment. However, these drugs can only alleviate AD symptoms. Thus, this research focuses on the discovery of novel lead compounds that possess multitarget regulation of AD etiopathology relating to amyloid cascade. The ascorbic acid structure has been designated as a core functional domain due to several characteristics, including antioxidant activities, amyloid aggregation inhibition, and the ability to be transported to the brain and neurons. Multifunctional ascorbic derivatives were synthesized by copper (I)-catalyzed azide–alkyne cycloaddition reaction (click chemistry). The in vitro and cell-based assays showed that compounds 2c and 5c exhibited prominent multifunctional activities as beta-secretase 1 inhibitors, amyloid aggregation inhibitors, and antioxidant, neuroprotectant, and anti-inflammatory agents. Significant changes in activities promoting neuroprotection and anti-inflammation were observed at a considerably low concentration at a nanomolar level. Moreover, an in silico study showed that compounds 2c and 5c were capable of being permeated across the blood–brain barrier by sodium-dependent vitamin C transporter-2.

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Ciaramelli, Carlotta, Alessandro Palmioli, Ada De Luigi, et al. "NMR-driven identification of anti-amyloidogenic compounds in green and roasted coffee extracts." Food Chemistry 252 (June 2018): 171–80. http://dx.doi.org/10.1016/j.foodchem.2018.01.075.

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Thèses sur le sujet "Anti-amyloidogenic compounds"

SIRONI, ERIKA. "Nuclear Magnetic Resonance characterization of Beta-amyloid peptides and their interactions with anti-amyloidogenic compounds." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2013. http://hdl.handle.net/10281/41573.

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Neurotoxic aggregates generated by amyloid beta peptides (Abeta) represent one of the main pathological features of Alzheimer’s Disease (AD). Nowadays many natural and synthetic compounds able to prevent Abeta peptide toxicity and aggregation have already been identified. Several of these compounds are not soluble in water, are chemically unstable and/or show pharmacological activities not directly correlated to AD. Among these, tetracycline, rosmarinic acid and curcumin, were analyzed for their ability to bind Abeta peptides. For this purpose NMR spectroscopy has been mainly employed, with the support of other biophysical methodologies. Obtained the structural information related to those interactions, some derivatives of these molecules, with improved solubility and chemical stability, were synthesized and tested in order to generate new Abeta ligands, useful for the development of new potential diagnostic and therapeutic tools against Alzheimer’s Disease.

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