ArticleBMC biotechnology2011
Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates.
Article in BMC biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 60 citations in OpenAlex.
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- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Propagation of α-synuclein pathology: models, mechanisms and future goals.Molecular neurodegeneration advances · 2026Review
- Quantitative detection of amyloid fibrils using fluorescence resonance energy transfer between engineered yellow and cyan proteins.Protein science : a publication of the Protein Society · 2025Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Label-Free Characterization of Amyloids and Alpha-Synuclein Polymorphs by Exploiting Their Intrinsic Fluorescence Property.Analytical chemistry · 2022Article
- Two-Photon Absorption: An Open Door to the NIR-II Biological Window?Frontiers in chemistry · 2022Review
- Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.International journal of molecular sciences · 2021Article
- Discovery of sustainable drugs for Alzheimer's disease: cardanol-derived cholinesterase inhibitors with antioxidant and anti-amyloid properties.RSC medicinal chemistry · 2021Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.The protein journal · 2019Review
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- Stability of Therapeutic Enzymes: Challenges and Recent Advances.Advances in experimental medicine and biology · 2019Review
- Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.Chembiochem : a European journal of chemical biology · 2018Article
- Two-photon probes for in vivo multicolor microscopy of the structure and signals of brain cells.Brain structure & function · 2018Review
- Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.Biophysical journal · 2017Article
- Single cell imaging and quantification of TDP-43 and α-synuclein intercellular propagation.Scientific reports · 2017Article
- Brain omega-3 polyunsaturated fatty acids modulate microglia cell number and morphology in response to intracerebroventricular amyloid-β 1-40 in mice.Journal of neuroinflammation · 2016Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundFluorescent tags, including small organic molecules and fluorescent proteins, enable the localization of protein molecules in biomedical research experiments. However, the use of these labels may interfere with the formation of larger-scale protein structures such as amyloid aggregates. Therefore, we investigate the effects of some commonly used fluorescent tags on the morphologies of fibrils grown from the Alzheimer's disease-associated peptide Amyloid β 1-40 (Aβ40) and the Parkinson's disease-associated protein α-synuclein (αS).
resultsUsing transmission electron microscopy (TEM), we verify that N-terminal labeling of Aβ40 with AMCA, TAMRA, and Hilyte-Fluor 488 tags does not prevent the formation of protofibrils and amyloid fibrils of various widths. We also measure the two-photon action cross-section of Aβ40 labelled with Hilyte Fluor 488 and demonstrate that this tag is suitable for use with two-photon fluorescence techniques. Similarly, we find that Alexa Fluor 488 labelling of αS variant proteins near either the N or C terminus (position 9 or 130) does not interfere with the formation of amyloid and other types of αS fibrils. We also present TEM images of fibrils grown from αS C-terminally labelled with enhanced green fluorescent protein (EGFP). Near neutral pH, two types of αS-EGFP fibrils are observed via TEM, while denaturation of the EGFP tag leads to the formation of additional species.
conclusionsWe demonstrate that several small extrinsic fluorescent tags are compatible with studies of amyloid protein aggregation. However, although fibrils can be grown from αS labelled with EGFP, the conformation of the fluorescent protein tag affects the observed aggregate morphologies. Thus, our results should assist researchers with label selection and optimization of solution conditions for aggregation studies involving fluorescence techniques.
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