scholarly journals Structure-Toxicity Relationships of Amyloid Peptide Oligomers

10.5772/30503 ◽  
2011 ◽  
Author(s):  
Patrick Walsh ◽  
Simon Sharpe
Keyword(s):  
Amyloid Peptide

Grape Seeds Extract as Brain Food: A Review

2017 ◽  
Vol 9 (1) ◽  
Author(s):  
Souad El Gengaihi ◽  
Doha H. Abou Baker
Keyword(s):  
Antioxidant Activities ◽  
Complex Mixture ◽  
Grape Seed Extract ◽  
Grape Seed ◽  
Seed Extract ◽  
Amyloid Peptide ◽  
Grape Seeds ◽  
Potential Benefits ◽  
Reduced Risk

Interest in the biological role of bioactive compounds present in medicinal herbs has increased over the last years. Of particular interest are plants that have an anti-Alzheimer activities. Several plants can be useful for Alzheimer (AD) management. Such as these which have anti-inflammatory activity, acetylcholinesterase (AChE) inhibitory action, antiapoptotic, slow the aggregation of amyloid peptide and antioxidant activities. Grape seed extract (GSE) is a complex mixture of several compounds, mostly represented by polyphenols and flavonoids. Their consumption is safe and is recognized to exert several health benefits. GS flavonoids have been associated with the reduced risk of chronic diseases, we present some findings on the potential benefits of GSE for the treatment of AD.

scholarly journals SIRT1-Dependent Upregulation of BDNF in Human Microglia Challenged with Aβ: An Early but Transient Response Rescued by Melatonin

Biomedicines ◽  
2021 ◽  
Vol 9 (5) ◽  
pp. 466
Author(s):  
Grazia Ilaria Caruso ◽  
Simona Federica Spampinato ◽  
Giuseppe Costantino ◽  
Sara Merlo ◽  
Maria Angela Sortino
Keyword(s):  
Nuclear Localization ◽  
Inflammatory Markers ◽  
Nuclear Translocation ◽  
Adenosine Monophosphate ◽  
Selective Inhibition ◽  
Amyloid Peptide ◽  
Human Microglia ◽  
Microglial Cell Line ◽  
Early Effects ◽  
Β Amyloid Peptide

Microglia represent a first-line defense in the brain. However, in pathological conditions such as Alzheimer’s disease (AD), a pro-inflammatory switch may occur, leading to loss of protective functions. Using the human microglial cell line HMC3, we showed that exposure to low concentrations of β-amyloid peptide 1-42 (Aβ42; 0.2 μM) initially (6 h) upregulated anti-inflammatory markers interleukin (IL)-4, IL-13, and brain-derived neurotrophic factor (BDNF). BDNF increase was prevented by selective inhibition of SIRT1 with EX527 (2 μM). Accordingly, these early effects were accompanied by a significant Aβ42-induced increase of SIRT1 expression, nuclear localization, and activity. SIRT1 modulation involved adenosine monophosphate-regulated kinase (AMPK), which was promptly (30 min) phosphorylated by Aβ42, while the AMPK inhibitor BML-275 (2 μM) attenuated Aβ42-induced SIRT1 increase. Initially observed microglial responses appeared transient, as microglial features changed when exposure to Aβ42 was prolonged (0.2 μM for 72 h). While SIRT1 and BDNF levels were reduced, the expression of inflammatory markers IL-1β and tumor necrosis factor (TNF)-α increased. This coincided with a rise in NF-kB nuclear localization. The effects of melatonin (1 μM) on prolonged microglial exposure to Aβ42 were analyzed for their protective potential. Melatonin was able to prolong SIRT1 and BDNF upregulation, as well as to prevent NF-kB nuclear translocation and acetylation. These effects were sensitive to the melatonin receptor antagonist, luzindole (25 μM). In conclusion, our data define an early microglial defensive response to Aβ42, featuring SIRT1-mediated BDNF upregulation that can be exogenously modulated by melatonin, thus identifying an important target for neuroprotection.

scholarly journals Competition of Aβ amyloid peptide and apolipoprotein E for receptor-mediated endocytosis

1999 ◽  
Vol 40 (3) ◽  
pp. 447-455 ◽  
Author(s):  
Karl Winkler ◽  
Hubert Scharnagl ◽  
Ursula Tisljar ◽  
Heinz Hoschützky ◽  
Isolde Friedrich ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Peptide ◽  
Receptor Mediated Endocytosis ◽  
Aβ Amyloid

N2L, a novel lipoic acid-niacin dimer protects HT22 cells against β-amyloid peptide-induced damage through attenuating apoptosis

2019 ◽  
Vol 34 (6) ◽  
pp. 1761-1770 ◽  
Author(s):  
Rikang Wang ◽  
Lang Zhang ◽  
Rifang Liao ◽  
Qian Li ◽  
Rongbiao Pi ◽  
...  
Keyword(s):  
Lipoic Acid ◽  
Amyloid Peptide ◽  
Ht22 Cells ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Purification and tissue level of the beta-amyloid peptide precursor of rat brain

1991 ◽  
Vol 266 (13) ◽  
pp. 8464-8469
Author(s):  
A. Potempska ◽  
J. Styles ◽  
P. Mehta ◽  
K.S. Kim ◽  
D.L. Miller
Keyword(s):  
Rat Brain ◽  
Beta Amyloid ◽  
Tissue Level ◽  
Amyloid Peptide ◽  
Beta Amyloid Peptide ◽  
Peptide Precursor

scholarly journals Anti-Aggregation Property of Allicin by In Vitro and Molecular Docking Studies

2019 ◽  
Vol 13 ◽  
pp. 117906951986618 ◽  
Author(s):  
Suresh Kumar ◽  
Shivani Kumar ◽  
Heera Ram
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Docking ◽  
Molecular Interaction ◽  
Fibril Formation ◽  
Amyloid Peptide ◽  
Peptide Aggregation ◽  
Aβ Peptide ◽  
In Silico Studies

Amyloidogenesis is the process in which amyloid beta (Aβ) peptide aggregation results in plaque formation in central nervous system (CNS) are associated with many neurological diseases such as Alzheimer’s disease. The peptide aggregation initiated from peptide monomers results in formation of dimers, tetramers, fibrils, and protofibrils. The ability of allicin, a lipid-soluble volatile organosulfur biological compound, present in freshly crushed garlic ( Allium sativum L.) to inhibit fibril formation by the Aβ peptide in vitro was investigated in the present study. Inhibition of fibrillogenesis was measured by a Thioflavin T (ThT) fluorescence assay and visualized by transmission electron microscopy (TEM). The molecular interaction between allicin and Aβ peptide was also demonstrated by in silico studies. The results show that allicin strongly inhibited Aβ fibrils by 97% at 300 µM, compared with control (Aβ only) ( P < .001). These results were further validated by visual of fibril formation by transmission microscopy and molecular interaction of amyloid peptide with allicin by molecular docking. Aβ forms favourable hydrophobic interaction with Ile32, Met35, Val36, and Val39, and oxygen of allicin forms hydrogen bond with the amino acid residue Lys28. Allicin anti-amyloidogenic property suggests that this naturally occurring compound may have potential to ameliorate and prevent Alzheimer’s disease.

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