Induced conformational change on ferrocenyl-terminated alkyls and their application as transducers for label-free immunosensing of Alzheimer's disease biomarker

RSC Advances ◽  
2016 ◽  
Vol 6 (3) ◽  
pp. 2414-2421 ◽  
Author(s):  
Abdelmoneim Mars ◽  
Wicem Argoubi ◽  
Sami Ben Aoun ◽  
Noureddine Raouafi

ApoE Alzheimer's disease biomarker can be sensitively detected by a label-free platform using flexible ferrocene-terminated alkyl chains. The immunorecognition triggers conformational changes, which improve the rate constants of electron-transfer.

2016 ◽  
Vol 29 (3) ◽  
pp. 748-755 ◽  
Author(s):  
Waleed A. El-Said ◽  
Kawthar Abd El-Hameed ◽  
Nagwa Abo El-Maali ◽  
Hayam G. Sayyed

2017 ◽  
Vol 57 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Victor Bloniecki ◽  
Dag Aarsland ◽  
Kaj Blennow ◽  
Jeffrey Cummings ◽  
Farshad Falahati ◽  
...  

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Takayuki Suzuki ◽  
Kazuma Murakami ◽  
Naotaka Izuo ◽  
Toshiaki Kume ◽  
Akinori Akaike ◽  
...  

Oligomers of 40- or 42-mer amyloidβ-protein (Aβ40, Aβ42) cause cognitive decline and synaptic dysfunction in Alzheimer's disease. We proposed the importance of a turn at Glu22 and Asp23 of Aβ42 to induce its neurotoxicity through the formation of radicals. Recently, a novel deletion mutant at Glu22 (E22Δ) of Aβ42 was reported to accelerate oligomerization and synaptotoxicity. To investigate this mechanism, the effects of the E22Δ mutation in Aβ42 and Aβ40 on the transformation ofβ-sheets, radical production, and neurotoxicity were examined. Both mutants promotedβ-sheet transformation and the formation of radicals, while their neurotoxicity was negative. In contrast, E22P-Aβ42 with a turn at Glu22 and Asp23 exhibited potent neurotoxicity along with the ability to form radicals and potent synaptotoxicity. These data suggest that conformational change in E22Δ-Aβis similar to that in E22P-Aβ42 but not the same, since E22Δ-Aβ42 exhibited no cytotoxicity, unlike E22P-Aβ42 and wild-type Aβ42.


2015 ◽  
Vol 11 (7S_Part_7) ◽  
pp. P340-P340
Author(s):  
Henrietta Wellington ◽  
Ulrika Törnqvist ◽  
Erik Portelius ◽  
Ross W. Paterson ◽  
Nadia K. Magdalinou ◽  
...  

2012 ◽  
Vol 8 (4S_Part_2) ◽  
pp. P72-P72
Author(s):  
Kewei Chen ◽  
Adam Fleisher ◽  
Napatkamon Ayutyanont ◽  
Yakeel Quiroz ◽  
Sergio Alvarez ◽  
...  

2020 ◽  
Vol 16 (S5) ◽  
Author(s):  
Nicholas J Ashton ◽  
Antoine Leuzy ◽  
Thomas K Karikari ◽  
Alessandra Dodich ◽  
Marina Boccardi ◽  
...  

2020 ◽  
Vol 8 (1) ◽  
Author(s):  
Dominik Röhr ◽  
Baayla D. C. Boon ◽  
Martin Schuler ◽  
Kristin Kremer ◽  
Jeroen J. M. Hoozemans ◽  
...  

AbstractThe neuropathology of Alzheimer’s disease (AD) is characterized by hyperphosphorylated tau neurofibrillary tangles (NFTs) and amyloid-beta (Aβ) plaques. Aβ plaques are hypothesized to follow a development sequence starting with diffuse plaques, which evolve into more compact plaques and finally mature into the classic cored plaque type. A better molecular understanding of Aβ pathology is crucial, as the role of Aβ plaques in AD pathogenesis is under debate. Here, we studied the deposition and fibrillation of Aβ in different plaque types with label-free infrared and Raman imaging. Fourier-transform infrared (FTIR) and Raman imaging was performed on native snap-frozen brain tissue sections from AD cases and non-demented control cases. Subsequently, the scanned tissue was stained against Aβ and annotated for the different plaque types by an AD neuropathology expert. In total, 160 plaques (68 diffuse, 32 compact, and 60 classic cored plaques) were imaged with FTIR and the results of selected plaques were verified with Raman imaging. In diffuse plaques, we detect evidence of short antiparallel β-sheets, suggesting the presence of Aβ oligomers. Aβ fibrillation significantly increases alongside the proposed plaque development sequence. In classic cored plaques, we spatially resolve cores containing predominantly large parallel β-sheets, indicating Aβ fibrils. Combining label-free vibrational imaging and immunohistochemistry on brain tissue samples of AD and non-demented cases provides novel insight into the spatial distribution of the Aβ conformations in different plaque types. This way, we reconstruct the development process of Aβ plaques in human brain tissue, provide insight into Aβ fibrillation in the brain, and support the plaque development hypothesis.


2020 ◽  
Vol 16 (S10) ◽  
Author(s):  
Oriol Grau‐Rivera ◽  
Irene Navalpotro ◽  
Gonzalo Sánchez‐Benavides ◽  
Marc Suárez‐Calvet ◽  
Marta Milà‐Alomà ◽  
...  

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