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| Hauptseite > Publikationsdatenbank > Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of α-Synuclein > print |
| Hauptseite > Publikationsdatenbank > Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of α-Synuclein > print |
| 001 | 916056 | ||
| 005 | 20230224084249.0 | ||
| 024 | 7 | _ | |a 10.1021/acschemneuro.2c00465 |2 doi |
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| 037 | _ | _ | |a FZJ-2022-05902 |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Rafiei, Yasin |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of α-Synuclein |
| 260 | _ | _ | |a Washington, DC |c 2022 |b ACS Publ. |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1673522321_27089 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Natural compounds with anti-aggregation capacity are increasingly recognized as viable candidates against neurodegenerative diseases. Recently, the polyphenolic fraction of propolis (PFP), a complex bee product, has been shown to inhibit amyloid aggregation of a model protein especially in the nanosheet form. Here, we examine the aggregation-modulating effects of the PFP nanosheets on α-synuclein (α-syn), an intrinsically disordered protein involved in the pathogenesis of Parkinson's disease. Based on a range of biophysical data including intrinsic and extrinsic fluorescence, circular dichroism (CD) data, and nuclear magnetic resonance spectroscopy, we propose a model for the interaction of α-syn with PFP nanosheets, where the positively charged N-terminal and the middle non-amyloid component regions of α-syn act as the main binding sites with the negatively charged PFP nanosheets. The Thioflavin T (ThT) fluorescence, Congo red absorbance, and CD data reveal a prominent dose-dependent inhibitory effect of PFP nanosheets on α-syn amyloid aggregation, and the microscopy images and MTT assay data suggest that the PFP nanosheets redirect α-syn aggregation toward nontoxic off-pathway oligomers. When preformed α-syn amyloid fibrils are present, fluorescence images show co-localization of PFP nanosheets and ThT, further confirming the binding of PFP nanosheets with α-syn amyloid fibrils. Taken together, our results demonstrate the binding and anti-aggregation activity of PFP nanosheets in a disease-related protein system and propose them as potential nature-based tools for probing and targeting pathological protein aggregates in neurodegenerative diseases. |
| 536 | _ | _ | |a 5241 - Molecular Information Processing in Cellular Systems (POF4-524) |0 G:(DE-HGF)POF4-5241 |c POF4-524 |f POF IV |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de |
| 700 | 1 | _ | |a Salmani, Bahram |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Mirzaei-Behbahani, Behnaz |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Taleb, Mahshid |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Meratan, Ali Akbar |0 0000-0002-1428-3254 |b 4 |e Corresponding author |
| 700 | 1 | _ | |a Ramezani, Mohammad |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Nikfarjam, Nasser |0 0000-0002-5995-7734 |b 6 |
| 700 | 1 | _ | |a Becker, Stefan |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Rezaie Ghaleh, Nasrollah |0 P:(DE-Juel1)194492 |b 8 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acschemneuro.2c00465 |g Vol. 13, no. 22, p. 3168 - 3179 |0 PERI:(DE-600)2528493-9 |n 22 |p 3168 - 3179 |t ACS chemical neuroscience |v 13 |y 2022 |x 1948-7193 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/916056/files/Polyphenols-Based%20Nanosheets%20of%20Propolis%20Modulate%20Cytotoxic%20Amyloid%20Fibril%20Assembly%20of%20%CE%B1-Synuclein-1.pdf |
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