Microchip Circulation Drastically Accelerates Amyloid Aggregation of 1–42 β-amyloid Peptide from Felis catus

2017 ◽  
Vol 8 (11) ◽  
pp. 2558-2567 ◽  
Author(s):  
Witold Gospodarczyk ◽  
Maciej Kozak
Keyword(s):  
Felis Catus ◽  
Amyloid Peptide ◽  
Amyloid Aggregation ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Modulation of β-amyloid aggregation by graphene quantum dots

2019 ◽  
Vol 6 (6) ◽  
pp. 190271 ◽  
Author(s):  
Changliang Liu ◽  
Huan Huang ◽  
Lilusi Ma ◽  
Xiaocui Fang ◽  
Chen Wang ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Structural Changes ◽  
Graphene Quantum Dots ◽  
Amyloid Peptide ◽  
Therapeutic Drug ◽  
Amyloid Aggregation ◽  
Β Amyloid ◽  
Regulatory Effects ◽  
Β Amyloid Peptide

Misfolding and abnormal aggregation of β-amyloid peptide is associated with the onset and progress of Alzheimer's disease (AD). Therefore, modulating β-amyloid aggregation is critical for the treatment of AD. Herein, we studied the regulatory effects and mechanism of graphene quantum dots (GQDs) on 1–42 β-amyloid (Aβ 1–42 ) aggregation. GQDs displayed significant regulatory effects on the aggregation of Aβ 1–42 peptide as detected by thioflavin T (ThT) assay. Then, the changes of confirmations and structures induced by GQDs on the Aβ 1–42 aggregation were monitored by circular dichroism (CD), dynamic light scattering (DLS) and transmission electron microscope (TEM). The in vitro cytotoxicity experiments further demonstrated the feasibility of GQDs on the regulation of Aβ 1–42 aggregation. Meanwhile, the structural changes of a Aβ 1–42 /GQDs mixture in different pH revealed that electrostatic interaction was the major driving force in the co-assembly process of Aβ 1–42 and GQDs. The proposed mechanism of the regulatory effects of GQDs on the Aβ 1–42 aggregation was also deduced reasonably. This work not only demonstrated the potential feasibility of GQDs as therapeutic drug for AD but also clarified the regulatory mechanism of GQDs on the Aβ 1–42 aggregation.

Inhibition of β-amyloid Aggregation of Ugni molinae Extracts

2020 ◽  
Vol 26 (12) ◽  
pp. 1365-1376 ◽  
Author(s):  
Daniela Jara-Moreno ◽  
Ana L. Riveros ◽  
Andrés Barriga ◽  
Marcelo J. Kogan ◽  
Carla Delporte
Keyword(s):  
Polyphenolic Compounds ◽  
Amyloid Peptide ◽  
Chemical Analyses ◽  
Amyloid Aggregation ◽  
Electronic Microscopy ◽  
Phenolic Profile ◽  
Amyloid Aggregates ◽  
Β Amyloid ◽  
Β Amyloid Peptide ◽  
Ugni Molinae

The β-amyloid peptide (1-42) is a molecule capable of aggregating into neurotoxic structures that have been implicated as potential etiological factors of Alzheimer's Disease. The aim of this study was to evaluate the inhibition of β-amyloid aggregation of ethyl acetate and ethanolic extracts obtained from Ugni molinae leaves on neurotoxic actions of β-amyloid aggregates. Chemical analyses were carried out with the extracts in order to determine their phenolic profile and its quantification. Both extracts showed a tendency to reduce neuronal deaths caused by β-amyloid. This tendency was inversely proportional to the evaluated concentrations. Moreover, the effect of EAE and ETE on β-amyloid aggregation was studied by fluorimetric T Thioflavin assay and transmission electronic microscopy (TEM); the extracts showed a modulation in the aggregation process. Partly, it is believed that these effects can be attributed to the polyphenolic compounds present in the extracts.

Dual effect of chitosan-based nanoparticles on the inhibition of β-amyloid peptide aggregation and disintegration of the preformed fibrils

2019 ◽  
Vol 7 (21) ◽  
pp. 3362-3373 ◽  
Author(s):  
Anjali Jha ◽  
Vandana Ghormade ◽  
Henry Kolge ◽  
Kishore M. Paknikar
Keyword(s):  
Alzheimer’S Disease ◽  
Therapeutic Intervention ◽  
Chitosan Nanoparticles ◽  
Amyloid Peptide ◽  
Peptide Aggregation ◽  
Amyloid Aggregation ◽  
Dual Effect ◽  
Promising Candidate ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Chitosan nanoparticles are a promising candidate for therapeutic intervention against Alzheimer's disease. They inhibit amyloid aggregation and dissolve preformed fibrils.

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 Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide

2005 ◽  
Vol 14 (8) ◽  
pp. 2125-2131 ◽  
Author(s):  
Tony Christopeit ◽  
Peter Hortschansky ◽  
Volker Schroeckh ◽  
Karlheinz Gührs ◽  
Giorgia Zandomeneghi ◽  
...  
Keyword(s):  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Inhibitors of Fibril Formation and Cytotoxicity of β-Amyloid Peptide Composed of KLVFF Recognition Element and Flexible Hydrophilic Disrupting Element

2002 ◽  
Vol 290 (1) ◽  
pp. 121-124 ◽  
Author(s):  
Ken-ichi Watanabe ◽  
Kazuhiko Nakamura ◽  
Shingo Akikusa ◽  
Tomoko Okada ◽  
Masato Kodaka ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Amyloid Peptide ◽  
Recognition Element ◽  
Β Amyloid ◽  
Β Amyloid Peptide
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