ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2022
Characterization of Substrates and Surface-Enhancement in Atomic Force Microscopy Infrared Analysis of Amyloid Aggregates.
Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Antiamyloid Antibody Effects on Aβ-42 Protein Aggregates Profiled Using Nanospectroscopy.Chemical & biomedical imaging · 2026Article
- An analytical model of label-free nanoscale chemical imaging reveals avenues toward improved spatial resolution and sensitivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Phospholipids and Cholesterol Determine Molecular Mechanisms of Cytotoxicity of α-Synuclein Oligomers and Fibrils.ACS chemical neuroscience · 2024Article
- Nanoscale structural characterization of transthyretin aggregates formed at different time points of protein aggregation using atomic force microscopy-infrared spectroscopy.Protein science : a publication of the Protein Society · 2023Article
- Saturation of fatty acids in phosphatidic acid uniquely alters transthyretin stability changing morphology and toxicity of amyloid fibrils.Chemistry and physics of lipids · 2023Article
- AFM-IR for Nanoscale Chemical Characterization in Life Sciences: Recent Developments and Future Directions.ACS measurement science au · 2023Review
- Concentration of Phosphatidylserine Influence Rates of Insulin Aggregation and Toxicity of Amyloid Aggregates In Vitro.ACS chemical neuroscience · 2023Article
- Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1-42 aggregates.The FEBS journal · 2023Article
- Mechanistic Insights Gained by High Spatial Resolution Reactivity Mapping of Homogeneous and Heterogeneous (Electro)Catalysts.Chemical reviews · 2023Review
- Protein-to-lipid ratio uniquely changes the rate of lysozyme aggregation but does not significantly alter toxicity of mature protein aggregates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023Article
- Elucidation of the Effect of Phospholipid Charge on the Rate of Insulin Aggregation and Structure and Toxicity of Amyloid Fibrils.ACS omega · 2023Article
- Lipids uniquely alter secondary structure and toxicity of lysozyme aggregates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Charge of Phospholipids Determines the Rate of Lysozyme Aggregation but Not the Structure and Toxicity of Amyloid Aggregates.The journal of physical chemistry letters · 2022Article
- Solid-to-Liposome Conformational Transition of Phosphatidylcholine and Phosphatidylserine Probed by Atomic Force Microscopy, Infrared Spectroscopy, and Density Functional Theory Calculations.Analytical chemistry · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Atomic force microscopy infrared (AFM-IR) spectroscopy is an emerging analytical technique that can be used to probe the structural organization of specimens with nanometer spatial resolution. A growing body of evidence suggests that nanoscale structural analysis of very small (<10 nm) biological objects, such as viruses and amyloid aggregates, requires substrates that must fit strict criteria of low surface roughness and low IR background, simultaneously. In this study, we examine the suitability of a broad range of substrates commonly used in AFM and IR fields, and we determined that silicon, zinc sulfide, and calcium fluoride are the most ideal substrates for nanoscale imaging of amyloid oligomers, protein aggregates that are directly linked to the onset and progression of neurodegenerative diseases. Our data show that these substrates provide the lowest roughness and the lowest background in the 800-1800 cm
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Registered trials
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.