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Journal articles on the topic 'Antiamyloidogenic'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Benseny-Cases, Núria, Oxana Klementieva, and Josep Cladera. "Dendrimers antiamyloidogenic potential in neurodegenerative diseases." New J. Chem. 36, no. 2 (2012): 211–16. http://dx.doi.org/10.1039/c1nj20469f.

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2

Chauhan, Ved, Lina Ji, and Abha Chauhan. "P1-442: Antiamyloidogenic properties of gelsolin." Alzheimer's & Dementia 4 (July 2008): T349. http://dx.doi.org/10.1016/j.jalz.2008.05.1024.

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3

Bermejo-Bescós, Paloma, Sagrario Martín-Aragón, Karim L. Jiménez-Aliaga, Andrea Ortega, María Teresa Molina, Eduardo Buxaderas, Guillermo Orellana, and Aurelio G. Csákÿ. "In vitro antiamyloidogenic properties of 1,4-naphthoquinones." Biochemical and Biophysical Research Communications 400, no. 1 (September 2010): 169–74. http://dx.doi.org/10.1016/j.bbrc.2010.08.038.

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4

Yu, Kun-Hua, and Cheng-I. Lee. "Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress." Pharmaceutics 12, no. 11 (November 11, 2020): 1081. http://dx.doi.org/10.3390/pharmaceutics12111081.

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Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β peptide (Aβ) and α-synuclein. However, the disaggregating ability is unclear in PrP fibrils. In this study, we examined the amyloid fibril-disaggregating activity of quercetin on mouse prion protein (moPrP) and characterized quercetin-bound moPrP fibrils by imaging, proteinase resistance, hemolysis assay, cell viability, and cellular oxidative stress measurements. The results showed that quercetin treatment can disaggregate moPrP fibrils and lead to the formation of the proteinase-sensitive amorphous aggregates. Furthermore, quercetin-bound fibrils can reduce the membrane disruption of erythrocytes. Consequently, quercetin-bound fibrils cause less oxidative stress, and are less cytotoxic to neuroblastoma cells. The role of quercetin is distinct from the typical function of antiamyloidogenic drugs that inhibit the formation of amyloid fibrils. This study provides a solution for the development of antiamyloidogenic therapy.

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5

Khaengkhan, Parinda, Yuki Nishikaze, Tetsuhiro Niidome, Kenji Kanaori, Kunihiko Tajima, Masatoshi Ichida, Shigeharu Harada, Hachiro Sugimoto, and Kaeko Kamei. "Identification of an antiamyloidogenic substance from mulberry leaves." NeuroReport 20, no. 13 (August 2009): 1214–18. http://dx.doi.org/10.1097/wnr.0b013e32832fa645.

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6

Benseny-Cases, Nuria, Oxana Klementieva, and Josep Cladera. "ChemInform Abstract: Dendrimers Antiamyloidogenic Potential in Neurodegenerative Diseases." ChemInform 43, no. 22 (May 3, 2012): no. http://dx.doi.org/10.1002/chin.201222233.

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7

Pandini, Giuseppe, Vincenza Pace, Agata Copani, Sebastiano Squatrito, Danilo Milardi, and Riccardo Vigneri. "Insulin Has Multiple Antiamyloidogenic Effects on Human Neuronal Cells." Endocrinology 154, no. 1 (January 1, 2013): 375–87. http://dx.doi.org/10.1210/en.2012-1661.

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Alzheimer’s disease is increased in diabetic patients. A defective insulin activity on the brain has been hypothesized to contribute to the neuronal cell dysregulation leading to AD, but the mechanism is not clear. We analyzed the effect of insulin on several molecular steps of amyloid precursor protein (APP) processing and β-amyloid (Aβ) intracellular accumulation in a panel of human neuronal cells and in human embryonic kidney 293 cells overexpressing APP-695. The data indicate that insulin, via its own receptor and the phosphatidylinositol-3-kinase/AKT pathway, influences APP phosphorylation at different sites. This rapid-onset, dose-dependent effect lasts many hours and mainly concerns dephosphorylation at the APP-T668 site. This effect of insulin was confirmed also in a human cortical neuronal cell line and in rat primary neurons. Cell fractionation and immunofluorescence studies indicated that insulin-induced APP-T668 dephosphorylation prevents the translocation of the APP intracellular domain fragment into the nucleus. As a consequence, insulin increases the transcription of antiamyloidogenic proteins such as the insulin-degrading enzyme, involved in Aβ degradation, and α-secretase. In contrast, the transcripts of pro-amyloidogenic proteins such as APP, β-secretase, and glycogen synthase kinase (Gsk)-3β are decreased. Moreover, cell exposure to insulin favors the nonamyloidogenic, α-secretase-dependent APP-processing pathway and reduces Aβ40 and Aβ42 intracellular accumulation, promoting their release in the extracellular compartment. The latter effects of insulin are independent of both Gsk-3β phosphorylation and APP-T668 dephosphorylation, as indicated by experiments with Gsk-3β inhibitors and with cells transfected with the nonphosphorylatable mutated APP-T668A analog. In human neuronal cells, therefore, insulin may prevent Aβ formation and accumulation by multiple mechanisms, both Gsk-3β dependent and independent.

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8

Chemerovski-Glikman, Marina, Michal Richman, and Shai Rahimipour. "Structure-based study of antiamyloidogenic cyclic d,l-α-peptides." Tetrahedron 70, no. 42 (October 2014): 7639–44. http://dx.doi.org/10.1016/j.tet.2014.07.097.

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9

Zhao, Zijian, Ling Zhu, Haiyun Li, Peng Cheng, Jiaxi Peng, Yudan Yin, Yang Yang, Chen Wang, Zhiyuan Hu, and Yanlian Yang. "Antiamyloidogenic Activity of Aβ42-Binding Peptoid in Modulating Amyloid Oligomerization." Small 13, no. 1 (October 7, 2016): 1602857. http://dx.doi.org/10.1002/smll.201602857.

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10

Fortin, Jessica S., and Marie-Odile Benoit-Biancamano. "Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs." Canadian Journal of Physiology and Pharmacology 94, no. 1 (January 2016): 35–48. http://dx.doi.org/10.1139/cjpp-2015-0117.

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Nonsteroidal anti-inflammatory drugs (NSAIDs) constitute an important pharmacotherapeutic class that, over the past decade, have expanded in application to a panoply of medical conditions. They have been tested for neurodegenerative diseases such as Alzheimer’s to reduce inflammation and also in the attempt to abrogate amyloid deposition. However, the use of NSAIDs as aggregation inhibitors has not been extensively studied in pancreatic amyloid deposition. Pancreatic amyloidosis involves the misfolding of islet amyloid polypeptide (IAPP) and contributes to the progression of type-2 diabetes in humans and felines. To ascertain their antiamyloidogenic activity, several NSAIDs were tested using fluorometric thioflavin-T assays, circular dichroism, photo-induced cross-linking assays, and cell culture. Celecoxib, diclofenac, indomethacin, meloxicam, niflumic acid, nimesulide, phenylbutazone, piroxicam, sulindac, and tenoxicam reduced fibrillization at a molar ratio of 1:10. The circular dichroism spectra of diclofenac, piroxicam, and sulindac showed characteristic spectral signatures found in predominantly α-helical structures. The oligomerization of human IAPP was abrogated with diclofenac and sulindac at a molar ratio of 1:5. The cytotoxic effects of pre-incubated human IAPP on cultured INS-1 cells were noticeably reduced in the presence of diclofenac, meloxicam, phenylbutazone, sulindac, and tenoxicam at a molar ratio of 1:10. Our results demonstrate that NSAIDs can provide chemical scaffolds to generate new and promising antiamyloidogenic agents that can be used alone or as a coadjuvant therapy.

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11

Mueller-Steiner, Sarah, Yungui Zhou, Hideaki Arai, Erik D. Roberson, Binggui Sun, Jennifer Chen, Xin Wang, et al. "Antiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease." Neuron 51, no. 6 (September 2006): 703–14. http://dx.doi.org/10.1016/j.neuron.2006.07.027.

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12

ONO, K., Y. YOSHIIKE, A. TAKASHIMA, K. HASEGAWA, H. NAIKI, and M. YAMADA. "Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro." Experimental Neurology 189, no. 2 (October 2004): 380–92. http://dx.doi.org/10.1016/j.expneurol.2004.05.035.

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13

NAIKI, Hironobu, Kazuhiro HASEGAWA, Kenjiro ONO, and Masahito YAMADA. "A Search for Antiamyloidogenic Compounds Based on a Nucleation-Dependent Polymerization Model." YAKUGAKU ZASSHI 130, no. 4 (2010): 503–9. http://dx.doi.org/10.1248/yakushi.130.503.

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14

Colas, Julien, Natacha Chessel, Allaeddine Ouared, Emmanuelle Gruz-Gibelli, Pascale Marin, François R. Herrmann, and Armand Savioz. "Neuroprotection against Amyloid-β-Induced DNA Double-Strand Breaks Is Mediated by Multiple Retinoic Acid-Dependent Pathways." Neural Plasticity 2020 (March 20, 2020): 1–14. http://dx.doi.org/10.1155/2020/9369815.

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In this study, we have investigated the role of all-trans-retinoic acid (RA) as a neuroprotective agent against Aβ1-42-induced DNA double-strand breaks (DSBs) in neuronal SH-SY5Y and astrocytic DI TNC1 cell lines and in murine brain tissues, by single-cell gel electrophoresis. We showed that RA does not only repair Aβ1-42-induced DSBs, as already known, but also prevents their occurrence. This effect is independent of that of other antioxidants studied, such as vitamin C, and appears to be mediated, at least in part, by changes in expression, not of the RARα, but of the PPARβ/δ and of antiamyloidogenic proteins, such as ADAM10, implying a decreased production of endogenous Aβ. Whereas Aβ1-42 needs transcription and translation for DSB production, RA protects against Aβ1-42-induced DSBs at the posttranslational level through both the RARα/β/γ and PPARβ/δ receptors as demonstrated by using specific antagonists. Furthermore, it could be shown by a proximity ligation assay that the PPARβ/δ-RXR interactions, not the RARα/β/γ-RXR interactions, increased in the cells when a 10 min RA treatment was followed by a 20 min Aβ1-42 treatment. Thus, the PPARβ/δ receptor, known for its antiapoptotic function, might for these short-time treatments play a role in neuroprotection via PPARβ/δ-RXR heterodimerization and possibly expression of antiamyloidogenic genes. Overall, this study shows that RA can not only repair Aβ1-42-induced DSBs but also prevent them via the RARα/β/γ and PPARβ/δ receptors. It suggests that the RA-dependent pathways belong to an anti-DSB Adaptative Gene Expression (DSB-AGE) system that can be targeted by prevention strategies to preserve memory in Alzheimer’s disease and aging.

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15

Kim, Ju Eun, and Jae Yoon Leem. "Acetylcholinesterase Inhibitory Activity and Antiamyloidogenic Effect of Cercis chinensis Bunge Seed Ethanolic Extract." Korean Journal of Medicinal Crop Science 29, no. 5 (October 31, 2021): 337–44. http://dx.doi.org/10.7783/kjmcs.2021.29.5.337.

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16

Siposova, Katarina, Veronika Huntosova, Yulia Shlapa, Lenka Lenkavska, Mariana Macajova, Anatolii Belous, and Andrey Musatov. "Advances in the Study of Cerium Oxide Nanoparticles: New Insights into Antiamyloidogenic Activity." ACS Applied Bio Materials 2, no. 5 (March 30, 2019): 1884–96. http://dx.doi.org/10.1021/acsabm.8b00816.

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17

Gupta, Veer Bala, S. S. Indi, and K. S. J. Rao. "Garlic extract exhibits antiamyloidogenic activity on amyloid-beta fibrillogenesis: relevance to Alzheimer's disease." Phytotherapy Research 23, no. 1 (January 2009): 111–15. http://dx.doi.org/10.1002/ptr.2574.

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18

Pérez-Hernández, Jesús, Víctor Javier Zaldívar-Machorro, David Villanueva-Porras, Elisa Vega-Ávila, and Anahí Chavarría. "A Potential Alternative against Neurodegenerative Diseases: Phytodrugs." Oxidative Medicine and Cellular Longevity 2016 (2016): 1–19. http://dx.doi.org/10.1155/2016/8378613.

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Neurodegenerative diseases (ND) primarily affect the neurons in the human brain secondary to oxidative stress and neuroinflammation. ND are more common and have a disproportionate impact on countries with longer life expectancies and represent the fourth highest source of overall disease burden in the high-income countries. A large majority of the medicinal plant compounds, such as polyphenols, alkaloids, and terpenes, have therapeutic properties. Polyphenols are the most common active compounds in herbs and vegetables consumed by man. The biological bioactivity of polyphenols against neurodegeneration is mainly due to its antioxidant, anti-inflammatory, and antiamyloidogenic effects. Multiple scientific studies support the use of herbal medicine in the treatment of ND; however, relevant aspects are still pending to explore such as metabolic analysis, pharmacokinetics, and brain bioavailability.

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19

Ozawa, Daisaku, Ryo Nomura, P. Patrizia Mangione, Kazuhiro Hasegawa, Tadakazu Okoshi, Riccardo Porcari, Vittorio Bellotti, and Hironobu Naiki. "Antiamyloidogenic and proamyloidogenic chaperone effects of C-reactive protein and serum amyloid P component." Amyloid 24, sup1 (March 16, 2017): 28–29. http://dx.doi.org/10.1080/13506129.2017.1295943.

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20

Bhatia, Nidhi K., Priya Modi, Shilpa Sharma, and Shashank Deep. "Quercetin and Baicalein Act as Potent Antiamyloidogenic and Fibril Destabilizing Agents for SOD1 Fibrils." ACS Chemical Neuroscience 11, no. 8 (March 25, 2020): 1129–38. http://dx.doi.org/10.1021/acschemneuro.9b00677.

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21

Zga, N., Y. Papastamoulis, A. Toribio, T. Richard, J. C. Delaunay, P. Jeandet, J. H. Renault, J. P. Monti, J. M. Mérillon, and P. Waffo-Téguo. "Preparative purification of antiamyloidogenic stilbenoids from Vitis vinifera (Chardonnay) stems by centrifugal partition chromatography." Journal of Chromatography B 877, no. 10 (April 2009): 1000–1004. http://dx.doi.org/10.1016/j.jchromb.2009.02.026.

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22

Naiki, Hironobu, Kazuhiro Hasegawa, Kenjiro Ono, and Masahito Yamada. "ChemInform Abstract: A Search for Antiamyloidogenic Compounds Based on a Nucleation-Dependent Polymerization Model." ChemInform 41, no. 32 (July 23, 2010): no. http://dx.doi.org/10.1002/chin.201032277.

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23

Lee, Young-Jung, Dong-Young Choi, Yeo-Pyo Yun, Sang Bae Han, Hwan Mook Kim, Kiho Lee, Seok Hwa Choi, et al. "Ethanol Extract ofMagnolia officinalisPrevents Lipopolysaccharide-Induced Memory Deficiency via Its Antineuroinflammatory and Antiamyloidogenic Effects." Phytotherapy Research 27, no. 3 (May 25, 2012): 438–47. http://dx.doi.org/10.1002/ptr.4740.

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24

Das, Sucharita, Suchismita Datta, Agamani Ghosal, Nibedita Ray Chaudhuri, Geetanjali Sundaram, and Soumalee Basu. "Screening of BACE1 inhibitors with antiamyloidogenic activity: A study of flavonoids and flavonoid derivatives." Neuroscience Letters 792 (January 2023): 136965. http://dx.doi.org/10.1016/j.neulet.2022.136965.

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25

Kouakou, Hilaire Tanoh, Laurent Kouakou Kouakou, Alain Decendit, Alain Badoc, Gregory Da-Costa, Jean-Michel Merillon, and Pierre Waffo Teguo. "Preparative Purification of Delphinidin 3-0-sambubioside from Roselle (Hibiscus sabdariffa L.) Petals by fast Centrifugation Partition Chromatography." JOURNAL OF ADVANCES IN CHEMISTRY 6, no. 2 (September 9, 2010): 999–1004. http://dx.doi.org/10.24297/jac.v6i2.2628.

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Delphinidin 3-0-sambubioside, a Hibiscus anthocyanin, was isolated from MeOH/TFA dried flower of H. sabdariffa. Its purification on preparative scale was obtained by centrifugal partition chromatography (CPC) using the ternary biphasic solvent systems composed of ethyl acetate/1-butanol/water, acidified by 0.1% of TFA. Stationary phase was ethyl acetate/1-butanol/water (5:5:90; v/v). We tested 4 mobile phases and found that the system acetate/1-butanol/water (40:46:14; v/v) was the best to separate anthocyanin mentioned above. This support-free liquid-liquid chromatographic procedure made it possible to isolate delphinidin 3-0-sambubioside from flower of H. sabdariffa. The antiamyloidogenic activity of the isolated stilbenes was evaluated versus b-amyloid fibrils. delphinidin 3-0-sambubioside was found to be active with 67% inhibition at 10 mM.

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26

Pradhan, Nibedita, Koushik Debnath, Suman Mandal, Nihar R. Jana, and Nikhil R. Jana. "Antiamyloidogenic Chemical/Biochemical-Based Designed Nanoparticle as Artificial Chaperone for Efficient Inhibition of Protein Aggregation." Biomacromolecules 19, no. 6 (May 9, 2018): 1721–31. http://dx.doi.org/10.1021/acs.biomac.8b00671.

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27

Pappolla, M. A., Y. J. Chyan, B. Poeggeler, B. Frangione, G. Wilson, J. Ghiso, and R. J. Reiter. "An assessment of the antioxidant and the antiamyloidogenic properties of melatonin: implications for Alzheimer's disease." Journal of Neural Transmission 107, no. 2 (February 9, 2000): 203–31. http://dx.doi.org/10.1007/s007020050018.

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28

Pasinetti, Giulio Maria. "Cyclooxygenase as a Target for the Antiamyloidogenic Activities of Nonsteroidal Anti-Inflammatory Drugs in Alzheimer’s Disease." Neurosignals 11, no. 5 (2002): 293–97. http://dx.doi.org/10.1159/000067428.

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29

Richman, Michal, Sarah Wilk, Marina Chemerovski, Sebastian K. T. S. Wärmländer, Anna Wahlström, Astrid Gräslund, and Shai Rahimipour. "In Vitro and Mechanistic Studies of an Antiamyloidogenic Self-Assembled Cyclic d,l-α-Peptide Architecture." Journal of the American Chemical Society 135, no. 9 (February 19, 2013): 3474–84. http://dx.doi.org/10.1021/ja310064v.

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30

Bustos, Victor, Maria V. Pulina, Ashley Bispo, Alison Lam, Marc Flajolet, Fred S. Gorelick, and Paul Greengard. "Phosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion." Proceedings of the National Academy of Sciences 114, no. 27 (May 22, 2017): 7148–53. http://dx.doi.org/10.1073/pnas.1705240114.

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Presenilin 1 (PS1), the catalytic subunit of the γ-secretase complex, cleaves βCTF to produce Aβ. We have shown that PS1 regulates Aβ levels by a unique bifunctional mechanism. In addition to its known role as the catalytic subunit of the γ-secretase complex, selective phosphorylation of PS1 on Ser367 decreases Aβ levels by increasing βCTF degradation through autophagy. Here, we report the molecular mechanism by which PS1 modulates βCTF degradation. We show that PS1 phosphorylated at Ser367, but not nonphosphorylated PS1, interacts with Annexin A2, which, in turn, interacts with the lysosomal N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) Vamp8. Annexin A2 facilitates the binding of Vamp8 to the autophagosomal SNARE Syntaxin 17 to modulate the fusion of autophagosomes with lysosomes. Thus, PS1 phosphorylated at Ser367 has an antiamyloidogenic function, promoting autophagosome–lysosome fusion and increasing βCTF degradation. Drugs designed to increase the level of PS1 phosphorylated at Ser367 should be useful in the treatment of Alzheimer’s disease.

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31

Davinelli, Sergio, Nadia Sapere, Davide Zella, Renata Bracale, Mariano Intrieri, and Giovanni Scapagnini. "Pleiotropic Protective Effects of Phytochemicals in Alzheimer's Disease." Oxidative Medicine and Cellular Longevity 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/386527.

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Alzheimer’s disease (AD) is a severe chronic neurodegenerative disorder of the brain characterised by progressive impairment in memory and cognition. In the past years an intense research has aimed at dissecting the molecular events of AD. However, there is not an exhaustive knowledge about AD pathogenesis and a limited number of therapeutic options are available to treat this neurodegenerative disease. Consequently, considering the heterogeneity of AD, therapeutic agents acting on multiple levels of the pathology are needed. Recent findings suggest that phytochemicals compounds with neuroprotective features may be an important resources in the discovery of drug candidates against AD. In this paper we will describe some polyphenols and we will discuss their potential role as neuroprotective agents. Specifically, curcumin, catechins, and resveratrol beyond their antioxidant activity are also involved in antiamyloidogenic and anti-inflammatory mechanisms. We will focus on specific molecular targets of these selected phytochemical compounds highlighting the correlations between their neuroprotective functions and their potential therapeutic value in AD.

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32

Purgatorio, Rosa, Nicola Gambacorta, Marco Catto, Modesto de Candia, Leonardo Pisani, Alba Espargaró, Raimon Sabaté, Saverio Cellamare, Orazio Nicolotti, and Cosimo D. Altomare. "Pharmacophore Modeling and 3D-QSAR Study of Indole and Isatin Derivatives as Antiamyloidogenic Agents Targeting Alzheimer’s Disease." Molecules 25, no. 23 (December 7, 2020): 5773. http://dx.doi.org/10.3390/molecules25235773.

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Thirty-six novel indole-containing compounds, mainly 3-(2-phenylhydrazono) isatins and structurally related 1H-indole-3-carbaldehyde derivatives, were synthesized and assayed as inhibitors of beta amyloid (Aβ) aggregation, a hallmark of pathophysiology of Alzheimer’s disease. The newly synthesized molecules spanned their IC50 values from sub- to two-digit micromolar range, bearing further information into structure-activity relationships. Some of the new compounds showed interesting multitarget activity, by inhibiting monoamine oxidases A and B. A cell-based assay in tau overexpressing bacterial cells disclosed a promising additional activity of some derivatives against tau aggregation. The accumulated data of either about ninety published and thirty-six newly synthesized molecules were used to generate a pharmacophore hypothesis of antiamyloidogenic activity exerted in a wide range of potencies, satisfactorily discriminating the ‘active’ compounds from the ‘inactive’ (poorly active) ones. An atom-based 3D-QSAR model was also derived for about 80% of ‘active’ compounds, i.e., those achieving finite IC50 values lower than 100 μM. The 3D-QSAR model (encompassing 4 PLS factors), featuring acceptable predictive statistics either in the training set (n = 45, q2 = 0.596) and in the external test set (n = 14, r2ext = 0.695), usefully complemented the pharmacophore model by identifying the physicochemical features mainly correlated with the Aβ anti-aggregating potency of the indole and isatin derivatives studied herein.

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33

Hyung, S. J., A. S. DeToma, J. R. Brender, S. Lee, S. Vivekanandan, A. Kochi, J. S. Choi, A. Ramamoorthy, B. T. Ruotolo, and M. H. Lim. "Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid- species." Proceedings of the National Academy of Sciences 110, no. 10 (February 20, 2013): 3743–48. http://dx.doi.org/10.1073/pnas.1220326110.

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34

Zhang, Qian, Jing Liu, Xiaoyu Hu, Wei Wang, and Zhi Yuan. "In Vitro Studies on Accelerating the Degradation and Clearance of Amyloid-β Fibrils by an Antiamyloidogenic Peptide." ACS Macro Letters 4, no. 4 (March 9, 2015): 339–42. http://dx.doi.org/10.1021/acsmacrolett.5b00033.

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35

Taghavi, F., M. Habibi-Rezaei, M. Bohlooli, M. Farhadi, M. Goodarzi, S. Movaghati, P. Maghami, et al. "Antiamyloidogenic Effects of Ellagic Acid on Human Serum Albumin Fibril Formation Induced by Potassium Sorbate and Glucose." Journal of Molecular Recognition 29, no. 12 (August 12, 2016): 611–18. http://dx.doi.org/10.1002/jmr.2560.

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36

Torricelli, C., E. Capurro, A. Santucci, A. Paffetti, C. D’Ambrosio, A. Scaloni, E. Maioli, and A. Pacini. "Multiple plasma proteins control atrial natriuretic peptide (ANP) aggregation." Journal of Molecular Endocrinology 33, no. 2 (October 2004): 335–41. http://dx.doi.org/10.1677/jme.1.01530.

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We have recently demonstrated that human α-atrial natriuretic peptide (α-hANP), an amyloidogenic peptide responsible for isolated atrial amyloidosis, binds to a dimeric form of apo A-I belonging to small high-density lipoproteins (HDL). This binding phenomenon is considered a protective mechanism since it inhibits or strongly reduces the ANP aggregation process. The observation that plasma exhibits at least four times greater amyloid inhibitory activity than HDL prompted us to determine whether small HDL are the only ANP plasma-binding factors. After incubation of whole plasma with labelled ANP, the macromolecular complexes were subjected to two-dimensional gel electrophoresis followed by autoradiography. The results presented here provide novel evidence of additional binding proteins, in addition to apo A-I dimer, able to bind ANP in vitro and to prevent its aggregation. The mass spectrometry analysis of the radioactive spots identified them as albumin, α-1 antitrypsin, orosomucoid and apo A-IV-TTR complex. The putative impact of these findings in the amyloidogenic/antiamyloidogenic peptides network is discussed.

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37

Caillon, Lucie, Anais R. F. Hoffmann, Alexandra Botz, and Lucie Khemtemourian. "Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus." Journal of Diabetes Research 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/5639875.

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Human islet amyloid polypeptide (hIAPP) is the major component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus (T2DM). Mature hIAPP, a 37-aa peptide, is natively unfolded in its monomeric state but forms islet amyloid in T2DM. In common with other misfolded and aggregated proteins, amyloid formation involves aggregation of monomers of hIAPP into oligomers, fibrils, and ultimately mature amyloid deposits. hIAPP is coproduced and stored with insulin by the pancreatic isletβ-cells and is released in response to the stimuli that lead to insulin secretion. Accumulating evidence suggests that hIAPP amyloid deposits that accompany T2DM are not just an insignificant phenomenon derived from the disease progression but that hIAPP aggregation induces processes that impair the functionality and the viability ofβ-cells. In this review, we particularly focus on hIAPP structure, hIAPP aggregation, and hIAPP-membrane interactions. We will also discuss recent findings on the mechanism of hIAPP-membrane damage and on hIAPP-induced cell death. Finally, the development of successful antiamyloidogenic agents that prevent hIAPP fibril formation will be examined.

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38

Young, Sherri. "A Systematic Review of Antiamyloidogenic and Metal-Chelating Peptoids: Two Structural Motifs for the Treatment of Alzheimer’s Disease." Molecules 23, no. 2 (January 31, 2018): 296. http://dx.doi.org/10.3390/molecules23020296.

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Koshti, Bharti, Vivekshinh Kshtriya, Corinne Nardin, and Nidhi Gour. "Chemical Perspective of the Mechanism of Action of Antiamyloidogenic Compounds Using a Minimalistic Peptide as a Reductionist Model." ACS Chemical Neuroscience 12, no. 15 (July 15, 2021): 2851–64. http://dx.doi.org/10.1021/acschemneuro.1c00221.

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Jiménez-Aliaga, Karim, Paloma Bermejo-Bescós, Juana Benedí, and Sagrario Martín-Aragón. "Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells." Life Sciences 89, no. 25-26 (December 2011): 939–45. http://dx.doi.org/10.1016/j.lfs.2011.09.023.

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Pichla, Monika, Grzegorz Bartosz, and Izabela Sadowska-Bartosz. "The Antiaggregative and Antiamyloidogenic Properties of Nanoparticles: A Promising Tool for the Treatment and Diagnostics of Neurodegenerative Diseases." Oxidative Medicine and Cellular Longevity 2020 (October 13, 2020): 1–11. http://dx.doi.org/10.1155/2020/3534570.

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Due to the progressive aging of the society, the prevalence and socioeconomic burden of neurodegenerative diseases are predicted to rise. The most common neurodegenerative disorders nowadays, such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis, can be classified as proteinopathies. They can be either synucleinopathies, amyloidopathies, tauopathies, or TDP-43-related proteinopathies; thus, nanoparticles with a potential ability to inhibit pathological protein aggregation and/or degrade already existing aggregates can be a promising approach in the treatment of neurodegenerative diseases. As it turns out, nanoparticles can be a double-edged sword; they can either promote or inhibit protein aggregation, depending on coating, shape, size, surface charge, and concentration. In this review, we aim to emphasize the need of a breakthrough in the treatment of neurodegenerative disorders and draw attention to nanomaterials, as they can also serve as a diagnostic tool for protein aggregates or can be used in a high-throughput screening for novel antiaggregative compounds.

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Kim, Jungsu, Adam E. M. Eltorai, Hong Jiang, Fan Liao, Philip B. Verghese, Jaekwang Kim, Floy R. Stewart, Jacob M. Basak, and David M. Holtzman. "Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis." Journal of Experimental Medicine 209, no. 12 (November 5, 2012): 2149–56. http://dx.doi.org/10.1084/jem.20121274.

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The apolipoprotein E (APOE) ε4 allele is the strongest genetic risk factor for Alzheimer’s disease (AD). The influence of apoE on amyloid β (Aβ) accumulation may be the major mechanism by which apoE affects AD. ApoE interacts with Aβ and facilitates Aβ fibrillogenesis in vitro. In addition, apoE is one of the protein components in plaques. We hypothesized that certain anti-apoE antibodies, similar to certain anti-Aβ antibodies, may have antiamyloidogenic effects by binding to apoE in the plaques and activating microglia-mediated amyloid clearance. To test this hypothesis, we developed several monoclonal anti-apoE antibodies. Among them, we administered HJ6.3 antibody intraperitoneally to 4-mo-old male APPswe/PS1ΔE9 mice weekly for 14 wk. HJ6.3 dramatically decreased amyloid deposition by 60–80% and significantly reduced insoluble Aβ40 and Aβ42 levels. Short-term treatment with HJ6.3 resulted in strong changes in microglial responses around Aβ plaques. Collectively, these results suggest that anti-apoE immunization may represent a novel AD therapeutic strategy and that other proteins involved in Aβ binding and aggregation might also be a target for immunotherapy. Our data also have important broader implications for other amyloidosis. Immunotherapy to proteins tightly associated with misfolded proteins might open up a new treatment option for many protein misfolding diseases.

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Azmi, Nur Hanisah, Maznah Ismail, Norsharina Ismail, Mustapha Umar Imam, Noorjahan Banu Mohammed Alitheen, and Maizaton Atmadini Abdullah. "Germinated Brown Rice Alters Aβ(1-42) Aggregation and Modulates Alzheimer’s Disease-Related Genes in Differentiated Human SH-SY5Y Cells." Evidence-Based Complementary and Alternative Medicine 2015 (2015): 1–12. http://dx.doi.org/10.1155/2015/153684.

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The pathogenesis of Alzheimer’s disease involves complex etiological factors, of which the deposition of beta-amyloid (Aβ) protein and oxidative stress have been strongly implicated. We explored the effects of H2O2, which is a precursor for highly reactive hydroxyl radicals, on neurotoxicity and genes related to AD on neuronal cells. Candidate bioactive compounds responsible for the effects were quantified using HPLC-DAD. Additionally, the effects of germinated brown rice (GBR) on the morphology of Aβ(1-42) were assessed by Transmission Electron Microscopy and its regulatory effects on gene expressions were explored. The results showed that GBR extract had several phenolic compounds andγ-oryzanol and altered the structure of Aβ(1-42) suggesting an antiamyloidogenic effect. GBR was also able to attenuate the oxidative effects of H2O2as implied by reduced LDH release and intracellular ROS generation. Furthermore, gene expression analyses showed that the neuroprotective effects of GBR were partly mediated through transcriptional regulation of multiple genes including Presenilins, APP, BACE1, BACE2, ADAM10, Neprilysin, and LRP1. Our findings showed that GBR exhibited neuroprotective properties via transcriptional regulation of APP metabolism with potential impact on Aβaggregation. These findings can have important implications for the management of neurodegenerative diseases like AD and are worth exploring further.

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Venkatesan, Ramu, Eunhee Ji, and Sun Yeou Kim. "Phytochemicals That Regulate Neurodegenerative Disease by Targeting Neurotrophins: A Comprehensive Review." BioMed Research International 2015 (2015): 1–22. http://dx.doi.org/10.1155/2015/814068.

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Alzheimer’s disease (AD), characterized by progressive dementia and deterioration of cognitive function, is an unsolved social and medical problem. Age, nutrition, and toxins are the most common causes of AD. However, currently no credible treatment is available for AD. Traditional herbs and phytochemicals may delay its onset and slow its progression and also allow recovery by targeting multiple pathological causes by antioxidative, anti-inflammatory, and antiamyloidogenic properties. They also regulate mitochondrial stress, apoptotic factors, free radical scavenging system, and neurotrophic factors. Neurotrophins such as BDNF, NGF, NT3, and NT4/5 play a vital role in neuronal and nonneuronal responses to AD. Neurotrophins depletion accelerates the progression of AD and therefore, replacing such neurotrophins may be a potential treatment for neurodegenerative disease. Here, we review the phytochemicals that mediate the signaling pathways involved in neuroprotection specifically neurotrophin-mediated activation of Trk receptors and members ofp75NTRsuperfamily. We focus on representative phenolic derivatives, iridoid glycosides, terpenoids, alkaloids, and steroidal saponins as regulators of neurotrophin-mediated neuroprotection. Although these phytochemicals have attracted attention owing to theirin vitroneurotrophin potentiating activity, theirin vivoand clinical efficacy trials has yet to be established. Therefore, further research is necessary to prove the neuroprotective effects in preclinical models and in humans.

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Naoi, Makoto, Masayo Shamoto-Nagai, and Wakako Maruyama. "Neuroprotection of multifunctional phytochemicals as novel therapeutic strategy for neurodegenerative disorders: antiapoptotic and antiamyloidogenic activities by modulation of cellular signal pathways." Future Neurology 14, no. 1 (February 2019): FNL9. http://dx.doi.org/10.2217/fnl-2018-0028.

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Uddin, Md Sahab, Abdullah Al Mamun, Md Motiar Rahman, Philippe Jeandet, Athanasios Alexiou, Tapan Behl, Md Shahid Sarwar, et al. "Natural Products for Neurodegeneration: Regulating Neurotrophic Signals." Oxidative Medicine and Cellular Longevity 2021 (June 21, 2021): 1–17. http://dx.doi.org/10.1155/2021/8820406.

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Neurodegenerative disorders (NDs) are heterogeneous groups of ailments typically characterized by progressive damage of the nervous system. Several drugs are used to treat NDs but they have only symptomatic benefits with various side effects. Numerous researches have been performed to prove the advantages of phytochemicals for the treatment of NDs. Furthermore, phytochemicals such as polyphenols might play a pivotal role in rescue from neurodegeneration due to their various effects as anti-inflammatory, antioxidative, and antiamyloidogenic agents by controlling apoptotic factors, neurotrophic factors (NTFs), free radical scavenging system, and mitochondrial stress. On the other hand, neurotrophins (NTs) including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), NT4/5, and NT3 might have a crucial neuroprotective role, and their diminution triggers the development of the NDs. Polyphenols can interfere directly with intracellular signaling molecules to alter brain activity. Several natural products also improve the biosynthesis of endogenous genes encoding antiapoptotic Bcl-2 as well as NTFs such as glial cell and brain-derived NTFs. Various epidemiological studies have demonstrated that the initiation of these genes could play an essential role in the neuroprotective function of dietary compounds. Hence, targeting NTs might represent a promising approach for the management of NDs. In this review, we focus on the natural product-mediated neurotrophic signal-modulating cascades, which are involved in the neuroprotective effects.

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Kashyap, Priya, Heera Ram, Sunil Dutt Shukla, and Suresh Kumar. "Scopoletin: Antiamyloidogenic, Anticholinesterase, and Neuroprotective Potential of a Natural Compound Present in Argyreia speciosa Roots by In Vitro and In Silico Study." Neuroscience Insights 15 (January 2020): 263310552093769. http://dx.doi.org/10.1177/2633105520937693.

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Alzheimer’s disease (AD) is characterized by depositions of amyloid β (Aβ) peptides aggregates resulting in plaques formation in the central nervous system (CNS). This study evaluates the disease-modifying potential of scopoletin against multiple factors associated with AD such as cholinesterase enzymes, Aβ peptides, and neuroprotective properties against Aβ- and H2O2-induced cytotoxicity under in vitro conditions. Scopoletin was identified and quantified using UPLC-QTOF (ultra-high performance liquid chromatography-quadrupole time-of-flight) and high-performance liquid chromatography (HPLC), respectively. The antiamyloidogenic potential was evaluated by thioflavin T and congo red binding assay. Inhibition of key enzymes, that is, acetylcholinesterase and butyrylcholinesterase, was investigated by Ellman’s assay. UPLC-QTOF analysis showed that most abundant phytoconstituent present in Argyreia speciosa hydroalcoholic root extract was scopoletin followed by festuclavine and ergometrine. Scopoletin was further quantified using novel reverse phase (RP)-HPLC method developed in this study. The neuroprotective potential of scopoletin was found to be 69% against Aβ42-induced neurotoxicity and 73% against H2O2-induced cytotoxicity in PC12 cell culture at 40 μM final concentration. At the same concentration, scopoletin inhibited Aβ42 fibril formation up to 57%. The IC50 concentration for AChE and BuChE enzyme inhibition by scopoletin was 5.34 and 9.11 μM, respectively. The antiaggregation and enzyme inhibition results were complemented with strong molecular interactions of scopoletin with target proteins validated by in silico molecular docking analysis. Based on this study, it can be concluded that scopoletin can be used as a lead for amelioration of symptoms and disease-modifying effects in AD.

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Chakraborty, Biswajit, Nobendu Mukerjee, Swastika Maitra, Mehrukh Zehravi, Dattatreya Mukherjee, Arabinda Ghosh, Ehab El Sayed Massoud, and Md Habibur Rahman. "Therapeutic Potential of Different Natural Products for the Treatment of Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2022 (July 22, 2022): 1–18. http://dx.doi.org/10.1155/2022/6873874.

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A high incidence of dementia (60–80%) and a high rate of memory loss are two of the most common symptoms of Alzheimer’s disease (AD), which affects the elderly. Researchers have recommended that traditional Chinese medicine (TCM) and Indian medicines can be used to prevent and cure AD. Several studies have linked neuroinflammation linked to amyloid-β (Aβ) deposition in the brain to the pathophysiology of neurodegenerative disorders. As a result, more research is needed to determine the role of inflammation in neurodegeneration. Increased microglial activation, cytokine production, reactive oxygen species (ROS), and nuclear factor kappa B (NF-κB) all play a role in the inflammatory process of AD. This review focuses on the role of neuroinflammation in neuroprotection and the molecular processes used by diverse natural substances, phytochemicals, and herbal formulations in distinct signaling pathways. Currently, researchers are focusing on pharmacologically active natural compounds with the anti-neuroinflammatory potential, making them a possible contender for treating AD. Furthermore, the researchers investigated the limits of past studies on TCM, Indian Ayurveda, and AD. Numerous studies have been carried out to examine the effects of medicinal whole-plant extracts on AD. Clinical investigations have shown that lignans, flavonoids, tannins, polyphenols, triterpenoids, sterols, and alkaloids have anti-inflammatory, antiamyloidogenic, anticholinesterase, and antioxidant properties. This review summarizes information about numerous medicinal plants and isolated compounds used in the treatment of AD and a list of further references.

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Suganthy, Natarajan, Vijayan Sri Ramkumar, Arivalagan Pugazhendhi, Giovanni Benelli, and Govindaraju Archunan. "Biogenic synthesis of gold nanoparticles from Terminalia arjuna bark extract: assessment of safety aspects and neuroprotective potential via antioxidant, anticholinesterase, and antiamyloidogenic effects." Environmental Science and Pollution Research 25, no. 11 (July 31, 2017): 10418–33. http://dx.doi.org/10.1007/s11356-017-9789-4.

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Forloni, Gianluigi. "Alzheimer’s disease: from basic science to precision medicine approach." BMJ Neurology Open 2, no. 2 (November 2020): e000079. http://dx.doi.org/10.1136/bmjno-2020-000079.

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Alzheimer’s disease (AD) is the most common form of dementia in the elderly. Together with cerebral amyloid accumulation, several factors contribute to AD pathology including vascular alterations, systemic inflammation, genetic/epigenetic status and mitochondrial dysfunction. Much is now being devoted to neuroinflammation. However, anti-inflammatory drugs as numerous other therapies, mainly targeted on β-amyloid, have failed to show efficacious effects in AD. Timing, proper selection of patients, and the need for a multitarget approach appear to be the main weak points of current therapeutic efforts. The efficacy of a treatment could be better evaluate if efficient biomarkers are available. We propose here the application of precision medicine principles in AD to simultaneously verify the efficacy of a treatment and the reliability of specific biomarkers according to individually tailored biomarker-guided targeted therapies. People at risk of developing AD or in the very early phase of the disease should be stratified according to: (1) neuropsychological tests; (2) apolipoprotein E (ApoE) genotyping; (3) biochemical analysis of plasma and cerebrospinal fluid (CSF); (4) MRI and positron emission tomography and (5) assessment of their inflammatory profile by an integration of various genetic and biochemical parameters in plasma, CSF and an analysis of microbiota composition. The selected population should be treated with antiamyloidogenic and anti-inflammatory drugs in randomised, longitudinal, placebo-controlled studies using ad hoc profiles (eg, vascular profile, mitochondrial profile, etc…) If these criteria are adopted widely and the results shared, it may be possible to rapidly develop innovative and personalised drug treatment protocols with more realistic chances of being efficacious.

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