scholarly journals S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation

2021 ◽  
Vol 22 (15) ◽  
pp. 7972
Author(s):  
Zigmantas Toleikis ◽  
Mantas Ziaunys ◽  
Lina Baranauskiene ◽  
Vytautas Petrauskas ◽  
Kristaps Jaudzems ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Amyloid Fibril ◽  
Alpha Synuclein ◽  
Aggregation Kinetics ◽  
Neuron Death ◽  
Force Microscopy ◽  
Atomic Force ◽  
Fibril Structure ◽  
Parkinson’S Diseases ◽  
Main Protein

The formation of amyloid fibril plaques in the brain creates inflammation and neuron death. This process is observed in neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases. Alpha-synuclein is the main protein found in neuronal inclusions of patients who have suffered from Parkinson’s disease. S100A9 is a calcium-binding, pro-inflammation protein, which is also found in such amyloid plaques. To understand the influence of S100A9 on the aggregation of α-synuclein, we analyzed their co-aggregation kinetics and the resulting amyloid fibril structure by Fourier-transform infrared spectroscopy and atomic force microscopy. We found that the presence of S100A9 alters the aggregation kinetics of α-synuclein and stabilizes the formation of a particular amyloid fibril structure. We also show that the solution’s ionic strength influences the interplay between S100A9 and α-synuclein, stabilizing a different structure of α-synuclein fibrils.

Atomic Force Microscopy: The Characterisation of Amyloid Protein Structure in Pathology

2020 ◽  
Vol 19 (32) ◽  
pp. 2958-2973 ◽  
Author(s):  
Maria J.E. Visser ◽  
Etheresia Pretorius
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Structure ◽  
Stimulated Emission ◽  
Laser Scanning Microscopy ◽  
Biological Research ◽  
Confocal Laser ◽  
Force Microscopy ◽  
Atomic Force ◽  
Parametric Data ◽  
Parkinson’S Diseases

: Proteins are versatile macromolecules that perform a variety of functions and participate in virtually all cellular processes. The functionality of a protein greatly depends on its structure and alterations may result in the development of diseases. Most well-known of these are protein misfolding disorders, which include Alzheimer’s and Parkinson’s diseases as well as type 2 diabetes mellitus, where soluble proteins transition into insoluble amyloid fibrils. Atomic Force Microscopy (AFM) is capable of providing a topographical map of the protein and/or its aggregates, as well as probing the nanomechanical properties of a sample. Moreover, AFM requires relatively simple sample preparation, which presents the possibility of combining this technique with other research modalities, such as confocal laser scanning microscopy, Raman spectroscopy and stimulated emission depletion microscopy. In this review, the basic principles of AFM are discussed, followed by a brief overview of how it has been applied in biological research. Finally, we focus specifically on its use as a characterisation method to study protein structure at the nanoscale in pathophysiological conditions, considering both molecules implicated in disease pathogenesis and the plasma protein fibrinogen. In conclusion, AFM is a userfriendly tool that supplies multi-parametric data, rendering it a most valuable technique.

2.305 The mechanism of alpha-synuclein fibril formation studied with high resolution Atomic Force Microscopy

2007 ◽  
Vol 13 ◽  
pp. S122-S123
Author(s):  
I. Segers-Nolten ◽  
G. Veldhuis ◽  
K. van der Werf ◽  
M. van Raaij ◽  
V. Subramaniam
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Alpha Synuclein ◽  
Fibril Formation ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Characterization of Alpha-Synuclein Early Aggregates by Atomic Force Microscopy

2010 ◽  
Vol 98 (3) ◽  
pp. 253a
Author(s):  
Jonathan Fauerbach ◽  
Dmytro Yushchenko ◽  
Alexander Demchenko ◽  
Thomas M. Jovin ◽  
Elizabeth A. Jares-Erijman
Keyword(s):  
Atomic Force Microscopy ◽  
Alpha Synuclein ◽  
Force Microscopy ◽  
Atomic Force

Multiscale fibril structure of hollow windmill palm fibers

2021 ◽  
pp. 004051752110051
Author(s):  
Changjie Chen ◽  
Zhong Wang ◽  
Sui Zhou ◽  
Guohe Wang ◽  
Limin Bao ◽  
...  
Keyword(s):  
Fiber Material ◽  
X Ray Diffraction ◽  
Palm Fiber ◽  
X Ray ◽  
Force Microscopy ◽  
Sulfuric Acid Treatment ◽  
Elementary Fibril ◽  
X Ray Scattering ◽  
Atomic Force ◽  
Fibril Structure

Windmill palm fiber is a kind of multicellular lignocellulose fiber material. Multiscale structure is an essential factor in mechanical properties and applications. The multiscale fibrils under sulfuric acid treatment had been prepared to improve the understanding of the macro-, micro-, and nanoscale structure of the windmill palm fiber. Scanning electron microscopy, atomic force microscopy, wide-angle X-ray scattering, and X-ray diffraction were used to analyze these samples’ structure. Furthermore, the result showed that the elementary fibril diameter was 4–10 nm, whereas that of the microfibrils was 20–70 nm. The diameters of macrofibril and macrofibril bundles were 0.4–1.0 µm and 1.2–5.5 µm, respectively. The elementary fibril assembled into spiral microfibril with an angle of 46°. The crystallinity of nanofibril extracted from windmill palm fiber was about 62%.

Atomic force microscopy and Kelvin probe force microscopy to study the mechanism of amyloid fibril formation and toxicity.

2012 ◽  
Vol 18 (S2) ◽  
pp. 884-885
Author(s):  
E. Drolle ◽  
F. Hane ◽  
Y. Choi ◽  
R. Gaikwad ◽  
S. Attwood ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Kelvin Probe Force Microscopy ◽  
Kelvin Probe ◽  
Force Microscopy ◽  
Atomic Force ◽  
Amyloid Fibril Formation

Extended abstract of a paper presented at Microscopy and Microanalysis 2012 in Phoenix, Arizona, USA, July 29 – August 2, 2012.

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.

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