An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled β-amyloid peptide fragments Aβ (31–35), Aβ (1–40) and Aβ (1–42)

2006 ◽  
Vol 50 (2) ◽  
pp. 104-111 ◽  
Author(s):  
Xiaojun Ji ◽  
David Naistat ◽  
Changqing Li ◽  
Jhony Orbulescu ◽  
Roger M. Leblanc
Keyword(s):  
Quantum Dots ◽  
Amyloid Fibrils ◽  
Amyloid Peptide ◽  
Peptide Fragments ◽  
Alternative Approach ◽  
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.

Synthesis and evaluation of arylquinones as BACE1 inhibitors, β-amyloid peptide aggregation inhibitors, and destabilizers of preformed β-amyloid fibrils

2011 ◽  
Vol 21 (8) ◽  
pp. 2183-2187 ◽  
Author(s):  
Andrea Ortega ◽  
Ángela Rincón ◽  
Karim L. Jiménez-Aliaga ◽  
Paloma Bermejo-Bescós ◽  
Sagrario Martín-Aragón ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Peptide ◽  
Peptide Aggregation ◽  
Aggregation Inhibitors ◽  
Β Amyloid ◽  
Β Amyloid Peptide

ChemInform Abstract: Synthesis and Evaluation of Arylquinones as BACE1 Inhibitors, β-Amyloid Peptide Aggregation Inhibitors, and Destabilizers of Preformed β-Amyloid Fibrils.

ChemInform ◽  
2011 ◽  
Vol 42 (34) ◽  
pp. no-no
Author(s):  
Andrea Ortega ◽  
Angela Rincon ◽  
Karim L. Jimenez-Aliaga ◽  
Paloma Bermejo-Bescos ◽  
Sagrario Martin-Aragon ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Peptide ◽  
Peptide Aggregation ◽  
Aggregation Inhibitors ◽  
Β Amyloid ◽  
Β Amyloid Peptide

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
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