ChemInform Abstract: The p3 Peptide, a Naturally Occurring Fragment of the Amyloid-β Peptide (Aβ) Found in Alzheimer′s Disease, Has a Greater Aggregation Propensity in vitro than Full-Length Aβ, but Does Not Bind Cu2+.

ChemInform ◽  
2000 ◽  
Vol 31 (45) ◽  
pp. no-no
Author(s):  
Feda Ali ◽  
Andrew J. Thompson ◽  
Colin J. Barrow
Keyword(s):  
Amyloid Β ◽  
Full Length ◽  
Amyloid Β Peptide ◽  
Aggregation Propensity ◽  
Naturally Occurring

Glycation induces conformational changes in the amyloid-β peptide and enhances its aggregation propensity: molecular insights

2016 ◽  
Vol 18 (46) ◽  
pp. 31446-31458 ◽  
Author(s):  
Asis K. Jana ◽  
Kedar B. Batkulwar ◽  
Mahesh J. Kulkarni ◽  
Neelanjana Sengupta
Keyword(s):  
Conformational Changes ◽  
In Silico ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Advanced Glycation ◽  
Aggregation Propensity

Underlying molecular insights into the higher aggregation propensity of the advanced glycation modified Aβ (or AGE-Aβ) from synchronizedin vitroandin silicostudies.

The p3 Peptide, a Naturally Occurring Fragment of the Amyloid-β Peptide (Aβ)Found in Alzheimer's Disease, Has a Greater Aggregation Propensity In Vitro Than Full-Length Aβ, But Does Not Bind Cu2+.

2000 ◽  
Vol 53 (4) ◽  
pp. 321 ◽  
Author(s):  
Feda Ali ◽  
Andrew J. Thompson ◽  
Colin J. Barrow
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Down's Syndrome ◽  
Amyloid Β ◽  
Down’S Syndrome ◽  
Full Length ◽  
Amyloid Β Peptide ◽  
Sheet Structure ◽  
Β Sheet

Cerebellar preamyloid from both Down’s syndrome and Alzheimer’s disease contains the p3 fragment (Aβ 17–40/42) as a major amyloid-β peptide (Aβ) component. The p3 peptide was previously shown to form amyloid in vitro, but less readily than full-length Aβ. Here we show that the p3 peptide has a greater β-sheet-forming propensity than full-length Aβ. Using circular dichroism spectroscopy we determined that in aqueous solutions the p3 peptide forms β-sheet structure more readily than full-length Aβ. The p3 peptide also has a lower α-helical propensity than full-length Aβ in the structure-forming solvent trifluoroethanol. These results indicate that the lower amyloidogenicity of the p3 peptide is not related to an inability to form β-sheet structure. In this study we also show that, unlike full-length Aβ, the p3 peptide does not bind Cu2+ ions. This inability to bind copper ions may explain why the p3 peptide appears to play a lesser role in Down’s syndrome and Alzheimer’s disease related neurodegeneration than does full-length Aβ.

Polyphenols from Traditional Chinese Medicine and Mediterranean Diet are effective against Aβ toxicity in vitro and in vivo in Caenorhabditis elegans

2022 ◽  
Author(s):  
Adriana Gea-González ◽  
Samanta Hernandez-Garcia ◽  
Paula Henarejos-Escudero ◽  
Pedro Martinez-Rodriguez ◽  
Francisco Garcia-Carmona ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Chinese Medicine ◽  
Traditional Chinese Medicine ◽  
Mediterranean Diet ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Naturally Occurring ◽  
Toxicity In Vitro

The potential of naturally-occurring polyphenols as nutraceuticals to prevent and/or treat Alzheimer’s disease is studied. Five structurally related flavones and four tyrosols were tested in vitro in human amyloid-β peptide...

Phenolic Acids Exert Anticholinesterase and Cognition-Improving Effects

2018 ◽  
Vol 15 (6) ◽  
pp. 531-543 ◽  
Author(s):  
Dominik Szwajgier ◽  
Ewa Baranowska-Wojcik ◽  
Kamila Borowiec
Keyword(s):  
Phenolic Acids ◽  
Ex Vivo ◽  
Amyloid Β ◽  
Inhibitory Effect ◽  
In Vivo Studies ◽  
Amyloid Β Peptide ◽  
Beneficial Effects ◽  
Aβ Fibrils

Numerous authors have provided evidence regarding the beneficial effects of phenolic acids and their derivatives against Alzheimer's disease (AD). In this review, the role of phenolic acids as inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) is discussed, including the structure-activity relationship. In addition, the inhibitory effect of phenolic acids on the formation of amyloid β-peptide (Aβ) fibrils is presented. We also cover the in vitro, ex vivo, and in vivo studies concerning the prevention and treatment of the cognitive enhancement.

scholarly journals Repeated electromagnetic field stimulation lowers amyloid-β peptide levels in primary human mixed brain tissue cultures

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Felipe P. Perez ◽  
Bryan Maloney ◽  
Nipun Chopra ◽  
Jorge J. Morisaki ◽  
Debomoy K. Lahiri
Keyword(s):  
Electromagnetic Field ◽  
Late Onset ◽  
Amyloid Β ◽  
Clinical Settings ◽  
Amyloid Β Peptide ◽  
Field Stimulation ◽  
Amino Acid Residues ◽  
Hyperphosphorylated Tau Protein ◽  
Magnetic Resonance Imaging Mri

AbstractLate Onset Alzheimer’s Disease is the most common cause of dementia, characterized by extracellular deposition of plaques primarily of amyloid-β (Aβ) peptide and tangles primarily of hyperphosphorylated tau protein. We present data to suggest a noninvasive strategy to decrease potentially toxic Aβ levels, using repeated electromagnetic field stimulation (REMFS) in primary human brain (PHB) cultures. We examined effects of REMFS on Aβ levels (Aβ40 and Aβ42, that are 40 or 42 amino acid residues in length, respectively) in PHB cultures at different frequencies, powers, and specific absorption rates (SAR). PHB cultures at day in vitro 7 (DIV7) treated with 64 MHz, and 1 hour daily for 14 days (DIV 21) had significantly reduced levels of secreted Aβ40 (p = 001) and Aβ42 (p = 0.029) peptides, compared to untreated cultures. PHB cultures (DIV7) treated at 64 MHz, for 1 or 2 hour during 14 days also produced significantly lower Aβ levels. PHB cultures (DIV28) treated with 64 MHz 1 hour/day during 4 or 8 days produced a similar significant reduction in Aβ40 levels. 0.4 W/kg was the minimum SAR required to produce a biological effect. Exposure did not result in cellular toxicity nor significant changes in secreted Aβ precursor protein-α (sAPPα) levels, suggesting the decrease in Aβ did not likely result from redirection toward the α-secretase pathway. EMF frequency and power used in our work is utilized in human magnetic resonance imaging (MRI, thus suggesting REMFS can be further developed in clinical settings to modulate Aβ deposition.

scholarly journals A cellular complex of BACE1 and γ-secretase sequentially generates Aβ from its full-length precursor

2019 ◽  
Vol 218 (2) ◽  
pp. 644-663 ◽  
Author(s):  
Lei Liu ◽  
Li Ding ◽  
Matteo Rovere ◽  
Michael S. Wolfe ◽  
Dennis J. Selkoe
Keyword(s):  
Molecular Weight ◽  
Cultured Cells ◽  
Amyloid Β ◽  
Full Length ◽  
Aβ Peptides ◽  
Whole Cells ◽  
Sequential Processing ◽  
Catalytically Active ◽  
Cellular Complex

Intramembrane proteolysis of transmembrane substrates by the presenilin–γ-secretase complex is preceded and regulated by shedding of the substrate’s ectodomain by α- or β-secretase. We asked whether β- and γ-secretases interact to mediate efficient sequential processing of APP, generating the amyloid β (Aβ) peptides that initiate Alzheimer’s disease. We describe a hitherto unrecognized multiprotease complex containing active β- and γ-secretases. BACE1 coimmunoprecipitated and cofractionated with γ-secretase in cultured cells and in mouse and human brain. An endogenous high molecular weight (HMW) complex (∼5 MD) containing β- and γ-secretases and holo-APP was catalytically active in vitro and generated a full array of Aβ peptides, with physiological Aβ42/40 ratios. The isolated complex responded properly to γ-secretase modulators. Alzheimer’s-causing mutations in presenilin altered the Aβ42/40 peptide ratio generated by the HMW β/γ-secretase complex indistinguishably from that observed in whole cells. Thus, Aβ is generated from holo-APP by a BACE1–γ-secretase complex that provides sequential, efficient RIP processing of full-length substrates to final products.

Effects of Hydrated Forms of C60 Fullerene on Amyloid β-Peptide Fibrillization In Vitro and Performance of the Cognitive Task

2007 ◽  
Vol 7 (4) ◽  
pp. 1479-1485 ◽  
Author(s):  
I. Ya. Podolski ◽  
Z. A. Podlubnaya ◽  
E. A. Kosenko ◽  
E. A. Mugantseva ◽  
E. G. Makarova ◽  
...  
Keyword(s):  
Cognitive Task ◽  
Amyloid Β ◽  
C60 Fullerene ◽  
Amyloid Β Peptide ◽  
And Performance

Gallotannins and Tannic Acid: First Chemical Syntheses and In Vitro Inhibitory Activity on Alzheimer’s Amyloid β-Peptide Aggregation

2015 ◽  
Vol 54 (28) ◽  
pp. 8217-8221 ◽  
Author(s):  
Tahiri Sylla ◽  
Laurent Pouységu ◽  
Grégory Da Costa ◽  
Denis Deffieux ◽  
Jean-Pierre Monti ◽  
...  
Keyword(s):  
Tannic Acid ◽  
Inhibitory Activity ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation
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