scholarly journals Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Rona Banerjee
Keyword(s):  
Atomic Force Microscopy ◽  
Ftir Spectroscopy ◽  
Amyloid Beta ◽  
Inhibitory Effect ◽  
Amyloid Beta Peptide ◽  
Inhibitory Effects ◽  
Force Microscopy ◽  
Mononuclear Complexes ◽  
Atomic Force ◽  
Beta Peptide

Mononuclear complexes of Curcumin with Cu(II) and Zn(II) have been synthesized and, characterized and their effects on the fibrillization and aggregation of amyloid-beta (Aβ) peptide have been studied. FTIR spectroscopy and atomic force microscopy (AFM) observations demonstrate that the complexes can inhibit the transition from less structured oligomers toβ-sheet rich protofibrils which act as seeding factors for further fibrillization. The metal complexes also impart more improved inhibitory effects than Curcumin on peptide fibrillization.

scholarly journals Effect of Varying Concentrations of Docosahexaenoic Acid on Amyloid Beta (1–42) Aggregation: An Atomic Force Microscopy Study

Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3089 ◽  
Author(s):  
Brenda Lee ◽  
Simon Attwood ◽  
Stephen Turnbull ◽  
Zoya Leonenko
Keyword(s):  
Atomic Force Microscopy ◽  
Docosahexaenoic Acid ◽  
Amyloid Beta ◽  
Amyloid Fibril ◽  
Inhibitory Effect ◽  
Fibril Formation ◽  
Force Microscopy ◽  
Atomic Force ◽  
Amyloid Fibril Formation ◽  
Fibril Length

Healthcare has advanced significantly, bringing with it longer life expectancies and a growing population of elders who suffer from dementia, specifically Alzheimer’s disease (AD). The amyloid beta (Aβ) peptide has been implicated in the cause of AD, where the peptides undergo a conformational change and form neurotoxic amyloid oligomers which cause neuronal cell death. While AD has no cure, preventative measures are being designed to either slow down or stop the progression of this neurodegenerative disease. One of these measures involves dietary supplements with polyunsaturated fatty acids such as docosahexaenoic acid (DHA). This omega-3 fatty acid is a key component of brain development and has been suggested to reduce the progression of cognitive decline. However, different studies have yielded different results as to whether DHA has positive, negative, or no effects on Aβ fibril formation. We believe that these discrepancies can be explained with varying concentrations of DHA. Here, we test the inhibitory effect of different concentrations of DHA on amyloid fibril formation using atomic force microscopy. Our results show that DHA has a strong inhibitory effect on Aβ1–42 fibril formation at lower concentrations (50% reduction in fibril length) than higher concentrations above its critical micelle concentration (70% increase in fibril length and three times the length of those at lower concentrations). We provide evidence that various concentrations of DHA can play a role in the inhibitory effects of amyloid fibril formation in vitro and help explain the discrepancies observed in previous studies.

Imaging real-time aggregation of amyloid beta protein (1–42) by atomic force microscopy

Peptides ◽  
2002 ◽  
Vol 23 (7) ◽  
pp. 1265-1270 ◽  
Author(s):  
Ashok Parbhu ◽  
Hai Lin ◽  
Julian Thimm ◽  
Ratneshwar Lal
Keyword(s):  
Atomic Force Microscopy ◽  
Real Time ◽  
Amyloid Beta ◽  
Amyloid Beta Protein ◽  
Force Microscopy ◽  
Time Aggregation ◽  
Atomic Force

scholarly journals Force clamp approach for characterization of nano-assembly in amyloid beta 42 dimer

Nanoscale ◽  
2019 ◽  
Vol 11 (25) ◽  
pp. 12259-12265 ◽  
Author(s):  
Sibaprasad Maity ◽  
Yuri L. Lyubchenko
Keyword(s):  
Atomic Force Microscopy ◽  
Amyloid Beta ◽  
Binding Pattern ◽  
Force Microscopy ◽  
Atomic Force ◽  
Force Clamp ◽  
Amyloid Beta 42

Atomic force microscopy force clamp approach was used for probing Aβ42 dimer that enabled us to measure stability and binding pattern within the dimer.

scholarly journals Conjugated Quantum Dots Inhibit the Amyloidβ(1–42) Fibrillation Process

2011 ◽  
Vol 2011 ◽  
pp. 1-15 ◽  
Author(s):  
Garima Thakur ◽  
Miodrag Micic ◽  
Yuehai Yang ◽  
Wenzhi Li ◽  
Dania Movia ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Quantum Dots ◽  
Atomic Force Microscopy ◽  
Amyloid Beta ◽  
Dihydrolipoic Acid ◽  
Force Microscopy ◽  
Atomic Force ◽  
Transmission Electron ◽  
Tht Fluorescence

Nanoparticles have enormous potential in diagnostic and therapeutic studies. We have demonstrated that the amyloid beta mixed with and conjugated to dihydrolipoic acid- (DHLA) capped CdSe/ZnS quantum dots (QDs) of size approximately 2.5 nm can be used to reduce the fibrillation process. Transmission electron microscopy (TEM) and atomic force microscopy (AFM) were used as tools for analysis of fibrillation. There is a significant change in morphology of fibrils when amyloidβ(1–42) (Aβ(1–42)) is mixed or conjugated to the QDs. The length and the width of the fibrils vary under modified conditions. Thioflavin T (ThT) fluorescence supports the decrease in fibril formation in presence of DHLA-capped QDs.

scholarly journals The Inhibitory Effect of Resveratrol on Elastin Amyloidogenesis

2014 ◽  
Vol 2014 ◽  
pp. 1-4
Author(s):  
Antonietta Pepe ◽  
Florian Delaunay ◽  
Angelo Bracalello ◽  
Brigida Bochicchio
Keyword(s):  
Molecular Structure ◽  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Inhibitory Effect ◽  
Degenerative Diseases ◽  
Force Microscopy ◽  
Atomic Force ◽  
Circular Dichroïsm

The role of polyphenols in the prevention of degenerative diseases is emerging in the last years. In this report, we will investigate in vitro the inhibitory effect of resveratrol on elastin amyloidogenesis. The effect of resveratrol on molecular structure was investigated by circular dichroism spectroscopy, while the inhibitory effect on self-assembly was evaluated by turbidimetry as a function of temperature and by atomic force microscopy.

scholarly journals Inhibitory effect of Cu(II)on Zn(II)-induced aggregation of amyloid beta peptide

2001 ◽  
Vol 41 (supplement) ◽  
pp. S44
Author(s):  
K. Suzuki ◽  
T. Miura ◽  
H. Takeuchi
Keyword(s):  
Amyloid Beta ◽  
Inhibitory Effect ◽  
Amyloid Beta Peptide ◽  
Beta Peptide ◽  
Induced Aggregation
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