scholarly journals Monitoring amyloid-β 42 conformational change using a spray-printed graphene electrode

2021 ◽  
Vol 123 ◽  
pp. 106927
Author(s):  
Bing Li ◽  
Guohui Zhang ◽  
Islam Bogachan Tahirbegi ◽  
Michael J. Morten ◽  
Haijie Tan
Keyword(s):  
Conformational Change ◽  
Amyloid Β ◽  
Graphene Electrode

Hydrophobicity and Conformational Change as Mechanistic Determinants for Nonspecific Modulators of Amyloid β Self-Assembly

Biochemistry ◽  
2011 ◽  
Vol 51 (1) ◽  
pp. 126-137 ◽  
Author(s):  
Axel Abelein ◽  
Benedetta Bolognesi ◽  
Christopher M. Dobson ◽  
Astrid Gräslund ◽  
Christofer Lendel
Keyword(s):  
Conformational Change ◽  
Self Assembly ◽  
Amyloid Β

Spike bursts increase amyloid-β 40/42 ratio by inducing a presenilin-1 conformational change

2013 ◽  
Vol 16 (5) ◽  
pp. 587-595 ◽  
Author(s):  
Iftach Dolev ◽  
Hilla Fogel ◽  
Hila Milshtein ◽  
Yevgeny Berdichevsky ◽  
Noa Lipstein ◽  
...  
Keyword(s):  
Conformational Change ◽  
Amyloid Β ◽  
Presenilin 1 ◽  
Spike Bursts

scholarly journals Early amyloid β-protein aggregation precedes conformational change

2014 ◽  
Vol 50 (40) ◽  
pp. 5373-5375 ◽  
Author(s):  
Bogdan Barz ◽  
Olujide O. Olubiyi ◽  
Birgit Strodel
Keyword(s):  
Molecular Dynamics ◽  
Protein Aggregation ◽  
Molecular Dynamics Simulations ◽  
Conformational Change ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Dynamics Simulations

The aggregation of amyloid-β protein (1–42) is studied at experimental concentrations using all-atom molecular dynamics simulations.

Template Induced Conformational Change of Amyloid-β Monomer

2012 ◽  
Vol 116 (25) ◽  
pp. 7398-7405 ◽  
Author(s):  
Wenhui Xi ◽  
Wenfei Li ◽  
Wei Wang
Keyword(s):  
Conformational Change ◽  
Amyloid Β

scholarly journals Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13

2006 ◽  
Vol 397 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Mike P. Williamson ◽  
Yu Suzuki ◽  
Nathan T. Bourne ◽  
Tetsuo Asakura
Keyword(s):  
Conformational Change ◽  
Conformational Changes ◽  
Senile Plaques ◽  
Amyloid Β ◽  
Sialic Acid Residue ◽  
Terminal Region ◽  
Random Coil ◽  
Neuronal Membrane ◽  
Amyloid Β Peptide ◽  
Surface Binding

Amyloid β-peptide (Aβ) is a major component of plaques in Alzheimer's disease, and formation of senile plaques has been suggested to originate from regions of neuronal membrane rich in gangliosides. Here we demonstrate using NMR on 15N-labelled Aβ-(1–40) and Aβ-(1–42) that the interaction with ganglioside GM1 micelles is localized to the N-terminal region of the peptide, particularly residues His13 to Leu17, which become more helical when bound. The key interaction is with His13, which undergoes a GM1-specific conformational change. The sialic acid residue of the ganglioside headgroup is important for determining the nature of the conformational change. The isolated pentasaccharide headgroup of GM1 is not bound, suggesting the need for a polyanionic surface. Binding to heparin confirms this suggestion, since binding is of similar affinity but does not produce the same conformational changes in the peptide. A comparison of Aβ-(1–40) and Aβ-(1–42) indicates that binding to GM1 micelles is not related to oligomerization, which occurs at the C-terminal end. These results imply that binding to ganglioside micelles causes a transition from random coil to α-helix in the N-terminal region, leaving the C-terminal region unstructured.

scholarly journals Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Yuhei Tachi ◽  
Yuko Okamoto ◽  
Hisashi Okumura
Keyword(s):  
Conformational Change ◽  
Amyloid Β

Amyloid β-peptide and Alzheimer's disease

2014 ◽  
Vol 56 ◽  
pp. 99-110 ◽  
Author(s):  
David Allsop ◽  
Jennifer Mayes
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Senile Plaques ◽  
Strong Support ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Cascade Hypothesis ◽  
Sequence Of Events ◽  
Aβ Amyloid ◽  
Amyloid Cascade

One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

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