Single-Molecule Kinetic Observation of Antibody Interactions with Growing Amyloid β Fibrils DOI Creative Commons
Maho Yagi‐Utsumi,

Yui Kanaoka,

Shigeyuki Miyajima

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(46), P. 31518 - 31528

Published: Oct. 24, 2024

Understanding the dynamic assembly process of amyloid β (Aβ) during fibril formation is essential for developing effective therapeutic strategies against Alzheimer's disease. Here, we employed high-speed atomic force microscopy to observe growth Aβ fibrils at single-molecule level, focusing specifically on their interaction with anti-Aβ antibodies. Our findings show that consists intermittent periods elongation and pausing, which are dictated by alternating addition monomers protofilaments. We highlight distinctive antibody 4396C, binds ends in paused state, suggesting a unique mechanism hinder elongation. Through real-time visualization interactions combined molecular simulation, this study provides refined understanding suggests novel therapy aimed inhibiting

Language: Английский

Clinical Importance of Amyloid Beta Implication in the Detection and Treatment of Alzheimer’s Disease DOI Open Access

Justyna Pokrzyk,

Agnieszka Kulczynska‐Przybik, Ewa M. Guzik-Makaruk

et al.

International Journal of Molecular Sciences, Journal Year: 2025, Volume and Issue: 26(5), P. 1935 - 1935

Published: Feb. 24, 2025

The role of amyloid beta peptide (Aβ) in memory regulation has been a subject substantial interest and debate neuroscience, because both physiological clinical issues. Understanding the dual nature Aβ is crucial for developing effective treatments Alzheimer's disease (AD). Moreover, accurate detection quantification methods isoforms have tested diagnostic purposes therapeutic interventions. This review provides insight into current knowledge about vivo vitro by fluid tests brain imaging (PET), which allow preclinical recognition disease. Currently, priority development new therapies given to potential changes progression In light increasing amounts data, this was focused on employment

Language: Английский

Citations

0

Functionalized carbon dots with guanidine salt ionic liquid regulate oxidative damage and amyloid aggregation DOI
Chao Wang, Tongtong Hou, Xu Shao

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 306, P. 141531 - 141531

Published: Feb. 26, 2025

Language: Английский

Citations

0

In Vivo Seeding of Amyloid-β Protein and Implications in Modeling Alzheimer’s Disease Pathology DOI Creative Commons
Qing Liu,

Simin Song,

Lu Liu

et al.

Biomolecules, Journal Year: 2025, Volume and Issue: 15(4), P. 571 - 571

Published: April 11, 2025

Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by extracellular plaques containing amyloid β-protein (Aβ) and intracellular neurofibrillary tangles formed tau. Cerebral Aβ accumulation initiates noxious cascade that leads to irreversible neuronal degeneration memory impairment in older adults. Recent advances seeding studies offer promising avenue for exploring the mechanisms underlying deposition complex pathological features of AD. However, extent which inoculated seeds can induce reproducible reliable manifestations remains unclear due significant variability across studies. In this review, we will discuss several factors contribute induction or acceleration consequent pathologies. Specifically, focus on diversity host animals, sources recipe seeds, inoculating strategies. By integrating these key aspects, review aims comprehensive perspective AD provide guidance modeling pathogenesis through exogenous introduction seeds.

Language: Английский

Citations

0

Single-Molecule Kinetic Observation of Antibody Interactions with Growing Amyloid β Fibrils DOI Creative Commons
Maho Yagi‐Utsumi,

Yui Kanaoka,

Shigeyuki Miyajima

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(46), P. 31518 - 31528

Published: Oct. 24, 2024

Understanding the dynamic assembly process of amyloid β (Aβ) during fibril formation is essential for developing effective therapeutic strategies against Alzheimer's disease. Here, we employed high-speed atomic force microscopy to observe growth Aβ fibrils at single-molecule level, focusing specifically on their interaction with anti-Aβ antibodies. Our findings show that consists intermittent periods elongation and pausing, which are dictated by alternating addition monomers protofilaments. We highlight distinctive antibody 4396C, binds ends in paused state, suggesting a unique mechanism hinder elongation. Through real-time visualization interactions combined molecular simulation, this study provides refined understanding suggests novel therapy aimed inhibiting

Language: Английский

Citations

2