ReviewCurrent pharmaceutical design2016
AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.
Review in Current pharmaceutical design, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 91 citations in OpenAlex.
- Single-Oligomer Characterization of Tau Phosphorylation and Mechanical State.ACS measurement science au · 2025Article
- Nanoscale Analysis beyond Imaging by Atomic Force Microscopy: Molecular Perspectives on Oncology and Neurodegeneration.Small science · 2025Review
- AFM for Studying the Functional Activity of Enzymes.Biomolecules · 2025Review
- Beta-Amyloid and Its Asp7 Isoform: Morphological and Aggregation Properties and Effects of Intracerebroventricular Administration.Brain sciences · 2024Article
- Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.Communications biology · 2024Article
- Enhanced surface nanoanalytics of transient biomolecular processes.Science advances · 2023Article
- Effects of β-amyloid (1-42) Administration on the Main Neurogenic Niches of the Adult Brain: Amyloid-Induced Neurodegeneration Influences Neurogenesis.International journal of molecular sciences · 2022Article
- Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- Force-Dependent Folding Kinetics of Single Molecules with Multiple Intermediates and Pathways.The journal of physical chemistry letters · 2022Article
- The Effect of Ethanol on Disassembly of Amyloid-βInternational journal of molecular sciences · 2022Article
- Generation of bispecific antibodies by structure-guided redesign of IgG constant regions.Frontiers in immunology · 2022Article
- Methods for the Characterization of Protein Aggregates.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Unraveling the Physicochemical Determinants of Protein Liquid-liquid Phase Separation by Nanoscale Infrared Vibrational Spectroscopy.Bio-protocol · 2021Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers.Nature communications · 2021Article
- Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers.International journal of molecular sciences · 2020Review
- Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.Nano letters · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA wide class of human diseases and neurodegenerative disorders, such as Alzheimer's disease, is due to the failure of a specific peptide or protein to keep its native functional conformational state and to undergo a conformational change into a misfolded state, triggering the formation of fibrillar cross-β sheet amyloid aggregates. During the fibrillization, several coexisting species are formed, giving rise to a highly heterogeneous mixture. Despite its fundamental role in biological function and malfunction, the mechanism of protein self-assembly and the fundamental origins of the connection between aggregation, cellular toxicity and the biochemistry of neurodegeneration remains challenging to elucidate in molecular detail. In particular, the nature of the specific state of proteins that is most prone to cause cytotoxicity is not established.
methodsIn the present review, we present the latest advances obtained by Atomic Force Microscopy (AFM) based techniques to unravel the biophysical properties of amyloid aggregates at the nanoscale. Unraveling amyloid single species biophysical properties still represents a formidable experimental challenge, mainly because of their nanoscale dimensions and heterogeneous nature. Bulk techniques, such as circular dichroism or infrared spectroscopy, are not able to characterize the heterogeneity and inner properties of amyloid aggregates at the single species level, preventing a profound investigation of the correlation between the biophysical properties and toxicity of the individual species.
conclusionThe information delivered by AFM based techniques could be central to study the aggregation pathway of proteins and to design molecules that could interfere with amyloid aggregation delaying the onset of misfolding diseases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.