Protective effects of β-sheet breaker α/β-hybrid peptide against amyloid β-induced neuronal apoptosis in vitro

2016 ◽  
Vol 89 (6) ◽  
pp. 888-900 ◽  
Author(s):  
Sourav Kumar ◽  
Ashim Paul ◽  
Sourav Kalita ◽  
Anup Kumar Ghosh ◽  
Bhubaneswar Mandal ◽  
...  
Keyword(s):  
Neuronal Apoptosis ◽  
Amyloid Β ◽  
Protective Effects ◽  
Hybrid Peptide ◽  
Β Sheet

Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide

2015 ◽  
Vol 51 (12) ◽  
pp. 2245-2248 ◽  
Author(s):  
Ashim Paul ◽  
Krishna Chaitanya Nadimpally ◽  
Tanmay Mondal ◽  
Kishore Thalluri ◽  
Bhubaneswar Mandal
Keyword(s):  
Anthranilic Acid ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation ◽  
Hybrid Peptide ◽  
Conformationally Restricted ◽  
Β Sheet

A novel class of anthranilic acid containing a conformationally restricted β-sheet breaker α/β-hybrid peptide efficiently disrupts preformed fibrillar aggregates of Aβ1–40in vitro.

Contrasting protective effects of cannabinoids against oxidative stress and amyloid-β evoked neurotoxicity in vitro

2012 ◽  
Vol 33 (1) ◽  
pp. 138-146 ◽  
Author(s):  
Benjamin S. Harvey ◽  
Katharina S. Ohlsson ◽  
Jesper L.V. Mååg ◽  
Ian F. Musgrave ◽  
Scott D. Smid
Keyword(s):  
Oxidative Stress ◽  
Amyloid Β ◽  
Protective Effects

scholarly journals Neuropharmacological Effects of Quercetin: A Literature-Based Review

2021 ◽  
Vol 12 ◽  
Author(s):  
Md. Shahazul Islam ◽  
Cristina Quispe ◽  
Rajib Hossain ◽  
Muhammad Torequl Islam ◽  
Ahmed Al-Harrasi ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Neuroprotective Effect ◽  
Animal Experiments ◽  
Amyloid Β ◽  
Neuronal Injury ◽  
Amyloid Β Peptide ◽  
Protective Effects ◽  
Neuroprotective Effects

Quercetin (QUR) is a natural bioactive flavonoid that has been lately very studied for its beneficial properties in many pathologies. Its neuroprotective effects have been demonstrated in many in vitro studies, as well as in vivo animal experiments and human trials. QUR protects the organism against neurotoxic chemicals and also can prevent the evolution and development of neuronal injury and neurodegeneration. The present work aimed to summarize the literature about the neuroprotective effect of QUR using known database sources. Besides, this review focuses on the assessment of the potential utilization of QUR as a complementary or alternative medicine for preventing and treating neurodegenerative diseases. An up-to-date search was conducted in PubMed, Science Direct and Google Scholar for published work dealing with the neuroprotective effects of QUR against neurotoxic chemicals or in neuronal injury, and in the treatment of neurodegenerative diseases. Findings suggest that QUR possess neuropharmacological protective effects in neurodegenerative brain disorders such as Alzheimer’s disease, Amyloid β peptide, Parkinson’s disease, Huntington's disease, multiple sclerosis, and amyotrophic lateral sclerosis. In summary, this review emphasizes the neuroprotective effects of QUR and its advantages in being used in complementary medicine for the prevention and treatment o of different neurodegenerative diseases.

scholarly journals Nanomedicine Against Aβ Aggregation by β–Sheet Breaker Peptide Delivery: In Vitro Evidence

Pharmaceutics ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 572 ◽  
Author(s):  
Pederzoli ◽  
Ruozi ◽  
Duskey ◽  
Hagmeyer ◽  
Sauer ◽  
...  
Keyword(s):  
Blood Brain Barrier ◽  
Polymeric Nanoparticles ◽  
Therapeutic Option ◽  
Amyloid Β ◽  
Peptide Delivery ◽  
Cellular Toxicity ◽  
Free Peptide ◽  
Aβ Aggregation ◽  
Β Sheet

The accumulation of amyloid β (Aβ) triggers a cascade of toxic events in Alzheimer’s disease (AD). The KLVFF peptide can interfere with Aβ aggregation. However, the peptide suffers from poor bioavailability and the inability to cross the blood–brain barrier. In this work, we study the possibility of adopting nanomedicine to overcome KLVFF limits in biodistribution. We produced new engineered polymeric nanoparticles (NPs), and we evaluated the cellular toxicity of these NPs and validated that KVLFF peptides released by NPs show the same promising effects on AD pathology. Our results revealed the successful generation of KVLFF loaded NPs that, without significant effects on cell heath, are even more potent in reversing Aβ-induced pathologies compared to the free peptide. Therefore, NPs will significantly advance KVLFF treatment as a therapeutic option for AD.

A Peptide Based Pro-Drug Ameliorates Amyloid-β Induced Neuronal Apoptosis in In Vitro SH-SY5Y Cells

2017 ◽  
Vol 14 (12) ◽  
Author(s):  
Sourav Kumar ◽  
Ashim Paul ◽  
Sourav Kalita ◽  
Awanish Kumar ◽  
Saurabh Srivastav ◽  
...  
Keyword(s):  
Neuronal Apoptosis ◽  
Amyloid Β

scholarly journals Protective Effects of Wu-Zi-Yan-Zong-Fang on Amyloid β-induced Damage In Vivo and In Vitro

2009 ◽  
Vol 129 (8) ◽  
pp. 941-948 ◽  
Author(s):  
Bin WANG ◽  
Xue Mei WANG ◽  
Hong FU ◽  
Geng Xin LIU
Keyword(s):  
Amyloid Β ◽  
Protective Effects

A Cationic Gallium Phthalocyanine Inhibits Amyloid β Peptide Fibril Formation

2020 ◽  
Vol 17 (7) ◽  
pp. 589-600
Author(s):  
Shatera Tabassum ◽  
Abdullah Md. Sheikh ◽  
Shozo Yano ◽  
Takahisa Ikeue ◽  
Shingo Mitaki ◽  
...  
Keyword(s):  
Near Infrared ◽  
Amyloid Β ◽  
Neuronal Cell ◽  
Fibril Formation ◽  
Lag Phase ◽  
Slice Culture ◽  
Amyloid Β Peptide ◽  
Protective Effects ◽  
Aβ Aggregation

Background: Amyloid β (Aβ) peptide deposition is considered as the main cause of Alzheimer’s disease (AD). Previously, we have shown that a Zn containing neutral phthalocyanine (Zn-Pc) inhibits Aβ fibril formation. Objective: The objective of this study is to investigate the effects of a cationic gallium containing Pc (GaCl-Pc) on Aβ fibril formation process. Methods and Results: Aβ fibril formation was induced by incubating synthetic Aβ peptides in a fibril forming buffer, and the amount of fibril was evaluated by ThT fluorescence assay. GaCl-Pc dosedependently inhibited both Aβ1-40 and Aβ1-42 fibril formation. It mainly inhibited the elongation phase of Aβ1-42 fibril formation kinetics, but not the lag phase. Western blotting results showed that it did not inhibit its oligomerization process, rather increased it. Additionally, GaCl-Pc destabilized preformed Aβ1- 42 fibrils dose-dependently in vitro condition, and decreased Aβ levels in the brain slice culture of APP transgenic AD model mice (J20 strain). Near-infrared scanning results showed that GaCl-Pc had the ability to bind to Aβ1-42. MTT assay demonstrated that GaCl-Pc did not have toxicity towards a neuronal cell line (A1) in culture rather, showed protective effects on Aβ-induced toxicity. Moreover, it dosedependently decreased Aβ-induced reactive oxygen species levels in A1 culture. Conclusion: Thus, our result demonstrated that GaCl-Pc decreased Aβ aggregation and destabilized the preformed fibrils. Since cationic molecules show a better ability to cross the blood-brain barrier, cationic GaCl-Pc could be important for the therapy of AD.

Tolfenamic Acid Prevents Amyloid β-induced Olfactory Bulb Dysfunction In Vivo

2018 ◽  
Vol 15 (8) ◽  
pp. 731-742 ◽  
Author(s):  
José M. Cornejo-Montes-de-Oca ◽  
Rebeca Hernández-Soto ◽  
Arturo G. Isla ◽  
Carlos E. Morado-Urbina ◽  
Fernando Peña-Ortega
Keyword(s):  
Olfactory Bulb ◽  
Amyloid Beta ◽  
Amyloid Β ◽  
Tolfenamic Acid ◽  
Network Activity ◽  
Protective Effects ◽  
Population Activity ◽  
Activity Inhibition

Background: Amyloid beta inhibits olfactory bulb function. The mechanisms involved in this effect must include alterations in network excitability, inflammation and the activation of different transduction pathways. Thus, here we tested whether tolfenamic acid, a drug that modulates several of these pathological processes, could prevent amyloid beta-induced olfactory bulb dysfunction. Objective: To test whether tolfenamic acid prevents amyloid beta-induced alterations in olfactory bulb network function, olfaction and GSK3β activity. Method: The protective effects of tolfenamic acid against amyloid beta-induced population activity inhibition were tested in olfactory bulb slices from adult mice, while tolfenamic acid and amyloid beta were bath-applied. We also tested the effects of amyloid-beta in slices obtained from animals pre-treated chronically (21 days) with tolfenamic acid. The effects of amyloid beta micro-injected into the olfactory bulbs were also tested, after two weeks, on olfactory bulb population activity and olfaction in control and tolfenamic acid chronically treated animals. Olfaction was assessed with the odor-avoidance and the habituation/cross-habituation tests. GSK3β activation was evaluated with Western-blot. Results: Acute bath application of tolfenamic acid does not prevent amyloid beta-induced inhibition of olfactory bulb network activity in vitro. In contrast, chronic treatment with tolfenamic acid renders the olfactory bulb resistant to amyloid beta-induced network activity inhibition in vitro and in vivo, which correlates with the inhibition of GSK3β activation and the protection against amyloid beta-induced olfactory dysfunction. Conclusion: Our data further support the use of tolfenamic acid to prevent amyloid beta-induced pathology and the early symptoms of Alzheimer Disease.

scholarly journals The Pluripotency Factor Nanog Protects against Neuronal Amyloid β-Induced Toxicity and Oxidative Stress through Insulin Sensitivity Restoration

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1339
Author(s):  
Ching-Chi Chang ◽  
Hsin-Hua Li ◽  
Sing-Hua Tsou ◽  
Hui-Chih Hung ◽  
Guang-Yaw Liu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Insulin Resistance ◽  
Stem Cell ◽  
Amyloid Β ◽  
Protective Effects ◽  
Mitochondrial Superoxide ◽  
Nanog Expression ◽  
Pluripotency Factor

Amyloid β (Aβ) is a peptide fragment of the amyloid precursor protein that triggers the progression of Alzheimer’s Disease (AD). It is believed that Aβ contributes to neurodegeneration in several ways, including mitochondria dysfunction, oxidative stress and brain insulin resistance. Therefore, protecting neurons from Aβ-induced neurotoxicity is an effective strategy for attenuating AD pathogenesis. Recently, applications of stem cell-based therapies have demonstrated the ability to reduce the progression and outcome of neurodegenerative diseases. Particularly, Nanog is recognized as a stem cell-related pluripotency factor that enhances self-renewing capacities and helps reduce the senescent phenotypes of aged neuronal cells. However, whether the upregulation of Nanog can be an effective approach to alleviate Aβ-induced neurotoxicity and senescence is not yet understood. In the present study, we transiently overexpressed Nanog—both in vitro and in vivo—and investigated the protective effects and underlying mechanisms against Aβ. We found that overexpression of Nanog is responsible for attenuating Aβ-triggered neuronal insulin resistance, which restores cell survival through reducing intracellular mitochondrial superoxide accumulation and cellular senescence. In addition, upregulation of Nanog expression appears to increase secretion of neurotrophic factors through activation of the Nrf2 antioxidant defense pathway. Furthermore, improvement of memory and learning were also observed in rat model of Aβ neurotoxicity mediated by upregulation of Nanog in the brain. Taken together, our study suggests a potential role for Nanog in attenuating the neurotoxic effects of Aβ, which in turn, suggests that strategies to enhance Nanog expression may be used as a novel intervention for reducing Aβ neurotoxicity in the AD brain.

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