scholarly journals Tau and Amyloid- Conformational Change to  -Sheet Structures as Effectors in the Development of Alzheimer's Disease

10.5772/37909 ◽  
2012 ◽  
Author(s):  
Martha A. De Anda-Hernndez ◽  
Karla I. Lira-De Len ◽  
Ral Mena ◽  
Victoria Campos-Pea ◽  
Marco A.
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Conformational Change

scholarly journals E22Δ Mutation in Amyloidβ-Protein Promotesβ-Sheet Transformation, Radical Production, and Synaptotoxicity, But Not Neurotoxicity

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Takayuki Suzuki ◽  
Kazuma Murakami ◽  
Naotaka Izuo ◽  
Toshiaki Kume ◽  
Akinori Akaike ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cognitive Decline ◽  
Conformational Change ◽  
Deletion Mutant ◽  
Protein A ◽  
Type A ◽  
Synaptic Dysfunction ◽  
Wild Type ◽  
Radical Production

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.

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
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Electron Transfer ◽  
Conformational Change ◽  
Conformational Changes ◽  
Rate Constants ◽  
Label Free ◽  
Alkyl Chains ◽  
Disease Biomarker

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.

Conformational change and GTPase activity of human tubulin: A comparative study on Alzheimer’s disease and healthy brain

2020 ◽  
Vol 155 (2) ◽  
pp. 207-224
Author(s):  
Shima Rajaei ◽  
Saeed Karima ◽  
Hessam Sepasi Tehrani ◽  
Somayeh Shateri ◽  
Somayeh Mahmoodi Baram ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Comparative Study ◽  
Conformational Change ◽  
Gtpase Activity

Aβ conformational change is central to Alzheimer’s disease

2002 ◽  
Vol 23 (6) ◽  
pp. 1085-1088 ◽  
Author(s):  
David M Holtzman
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Conformational Change

Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease

2005 ◽  
Vol 8 (1) ◽  
pp. 29-41 ◽  
Author(s):  
José Luna-Muñoz ◽  
Francisco García-Sierra ◽  
Viviana Falcón ◽  
Ivón Menéndez ◽  
Laura Chávez-Macías ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Structural Change ◽  
Conformational Change ◽  
Tau Protein

scholarly journals Synthesis and simulation of new cyclodextrin derivatives breaker for Aß42

2020 ◽  
Vol 9 (3) ◽  
pp. 117-120
Author(s):  
Assia Keniche ◽  
Katia ouled Taleb
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Conformational Change ◽  
Neurodegenerative Disorder ◽  
The Other ◽  
Cyclodextrin Derivatives ◽  
Recognition Sequence ◽  
Specific Recognition

The amyloid Ab-42, a peptide involved, following a conformational change in b sheets in the pathology of the main neurodegenerative disorder of Alzheimer's disease, is targeted in our study, the latter of which reports the synthesis of two Inhibitors linked to a specific recognition sequence synthesized during this work (Tryp-Val-Val-COOH), one linked to an aziridine and the other to a methylated β-CD in order to be able to stop the aggregation of the peptide involved.

scholarly journals Studies on Interaction of Buffalo Brain Cystatin with Donepezil: An Alzheimer's Drug

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Fakhra Amin ◽  
Bilqees Bano
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Conformational Change ◽  
Structural Changes ◽  
Gel Filtration ◽  
Alkaline Treatment ◽  
Uv Spectra ◽  
Cysteine Protease Inhibitor ◽  
Native Page ◽  
Ammonium Sulphate Fractionation

When drugs bind to a protein, the intramolecular structures can be altered, resulting in conformational change of the protein. Donepezil, an Acetyl Cholinesterase inhibitor (AChE), is commonly prescribed to patients with Alzheimer's disease (AD) to enhance cholinergic neurotransmission. It is the “first-line” agents in the treatment of Alzheimer's disease used to improve cognitive function in the disease. In the present study, a cysteine protease inhibitor (cystatin) has been isolated from buffalo brain using alkaline treatment, 40 to 60% ammonium sulphate fractionation and gel filtration chromatography on Sephadex G-75 with % yield of 64.13 and fold purification of 384.7. The purified inhibitor (Buffalo Brain Cystatin, (BBC)) was eluted as a single papain inhibitory peak which migrated as single band on native PAGE; however, on SDS-PAGE with and without beta mercaptoethanol (βME) BBC gave two bands of M W 31.6 and 12.4 KDa, respectively. The molecular weight determined by gel filtration came out to be 43.6 KDa. The UV spectra of cystatin on interaction with donepezil suggested a conformational change in the protein. The fluorescence spectra of BC-donepezil composite show structural changes indicating 40 nm red shift with significant increase in fluorescence intensity of cystatin in the presence of donepezil representing an unfolding of cystatin on interaction, which is an indication of side effect of donepezil during the use of this drug.

Cognitive control constrains memory attributions

2019 ◽  
Vol 42 ◽  
Author(s):  
Colleen M. Kelley ◽  
Larry L. Jacoby
Keyword(s):  
Alzheimer’S Disease ◽  
Older Adults ◽  
Alzheimer's Disease ◽  
Traumatic Brain Injury ◽  
Brain Injury ◽  
Cognitive Control

Abstract Cognitive control constrains retrieval processing and so restricts what comes to mind as input to the attribution system. We review evidence that older adults, patients with Alzheimer's disease, and people with traumatic brain injury exert less cognitive control during retrieval, and so are susceptible to memory misattributions in the form of dramatic levels of false remembering.

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