A FRET pair for quantitative and superresolution imaging of amyloid fibril formation

Ruiz-Arias, Álvaro; Jurado, Rocío; Fueyo-González, Francisco; Herranz, Rosario; Gálvez, Natividad; González‐Vera, Juan A.; Orte, Ángel

doi:10.1016/j.snb.2021.130882

Cited by 16 publications

(5 citation statements)

References 45 publications

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“…We can thus obtain the degree of acetylation per cell (FRET intensity value in each cell) as well as the average signal in the Foxp3+ compartment by measure the mean fluorescence intensity (MFI). Furthermore the apparent FRET efficiency per cell typically used in microscopy experiments 44 , 45 and defined as %FRET (intensity of the acceptor∗100/(intensity of the acceptor + intensity of the donor), can also be calculated in flow cytometry experiments. This measurement is less sensitive to noise and is corrected for spectral bleed-through in each channel using the corresponding singly-stained controls (see STAR Methods ).…”

Section: Resultsmentioning

confidence: 99%

Small-molecule TIP60 inhibitors enhance regulatory T cell induction through TIP60-P300 acetylation crosstalk

Fueyo-González,

Vilanova,

Ningoo

et al. 2023

iScience

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Section: Resultsmentioning

confidence: 99%

Small-molecule TIP60 inhibitors enhance regulatory T cell induction through TIP60-P300 acetylation crosstalk

Fueyo-González,

Vilanova,

Ningoo

et al. 2023

iScience

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“…For example, a super-resolution technique, like, stimulated fluorescence emission depletion (STED) in combination with fluorescence lifetime imaging microscopy (FLIM), has recently been used to track the structural details of apoferritin fibrils. 104 Broadly, the advantage of this technique lies in the capturing of super-resolution structures through selective deactivation of fluorophores using a highpower laser pulse, thereby enabling tracking of diffractionlimited regions through a reduction of the illumination spot. On the other hand, the same technique was also used to image the amyloid aggregates made up of α-synuclein with ThT as a fluorescent tag.…”

Section: Interaction Of Single Amino Acid-based Fibrils With Lipid Ve...mentioning

confidence: 99%

“…On the other hand, other than the conventional fluorescence microscope, the application of super-resolution imaging on amyloid fibrils helps to interrogate their structural motif with finer details. For example, a super-resolution technique, like, stimulated fluorescence emission depletion (STED) in combination with fluorescence lifetime imaging microscopy (FLIM), has recently been used to track the structural details of apoferritin fibrils . Broadly, the advantage of this technique lies in the capturing of super-resolution structures through selective deactivation of fluorophores using a high-power laser pulse, thereby enabling tracking of diffraction-limited regions through a reduction of the illumination spot.…”

Section: Interaction Of Single Amino Acid-based Fibrils With Lipid Ve...mentioning

confidence: 99%

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Interactions between Lipid Vesicle Membranes and Single Amino Acid Fibrils: Probable Origin of Specific Neurological Disorders

Nandi,

Sarkar

2024

Langmuir

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Amyloid fibrils are known to be responsible for several neurological disorders, like Alzheimer's disease (AD), Parkinson's disease (PD), etc. For decades, mostly proteins and peptide-based amyloid fibrils have been focused on, and the topic has acknowledged the rise, development, understanding of, and controversy, as well. However, the single amino acid based amyloid fibrils, responsible for several disorders, such as phenylketonuria, tyrosenimia type II, hypermethioninemia, etc., have gotten scientific attention lately. To understand the molecular level pathogenesis of such disorders originated due to the accumulation of single amino acid-based amyloid fibrils, interaction of these fibrils with phospholipid vesicle membranes is found to be an excellent cell-free in vitro setup. Based on such an in vitro setup, these fibrils show a generic mechanism of membrane insertion driven by electrostatic and hydrophobic effects inside the membrane that reduces the integral rigidity of the membrane. Alteration of such fundamental properties of the membrane, therefore, might be referred to as one of the prime pathological factors for the development of these neurological disorders. Hence, such interactions must be investigated in cellular and intracellular compartments to design suitable therapeutic modulators against fibrils.

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“…We utilized a time-lapse TAB 15 imaging protocol to visualize the remodeling of each amyloid fiber with nanoscale resolution. Specifically, we added the solvatochromic and fluorogenic dye Nile blue (NB) [41][42][43] to the imaging chambers after amyloid adsorption (Figure 1a), and "flashes" of NB fluorescence commensurate with binding to the fibril surfaces were captured by an x-and y-polarized microscope 40 (Figure S1). Typically, 10,000 images of NB blinking were recorded for each SMOLM reconstruction with a 20 ms exposure time under 637-nm illumination.…”

mentioning

confidence: 99%

Single-Molecule Orientation Imaging Reveals the Nano-Architecture of Amyloid Fibrils Undergoing Growth and Decay

Sun,

Ding,

Zhou

et al. 2024

Preprint

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Amyloid-beta (Aβ42) aggregates are characteristic signatures of Alzheimer's disease, but probing how their nanoscale architectures influence their growth and decay remains challenging using current technologies. Here, we apply time-lapse single-molecule orientation-localization microscopy (SMOLM) to measure the orientations and rotational "wobble" of Nile blue (NB) molecules transiently binding to Aβ42 fibrils. We quantify correlations between fibril architectures, measured by SMOLM, and their growth and decay visualized by single-molecule localization microscopy (SMLM). We discover that stable Aβ42 fibrils tend to be well-ordered, signified by well-aligned NB orientations and small wobble. SMOLM also shows that increasing order and disorder are signatures of growing and decaying Aβ42 fibrils, respectively. We also observe SMLM-invisible fibril remodeling, including steady growth and decay patterns that conserve β-sheet organization. SMOLM reveals that increased heterogeneity in fibril architectures is correlated with more dynamic remodeling and that large-scale fibril remodeling tends to originate from local regions that exhibit strong heterogeneity.

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A FRET pair for quantitative and superresolution imaging of amyloid fibril formation

Cited by 16 publications

References 45 publications

Small-molecule TIP60 inhibitors enhance regulatory T cell induction through TIP60-P300 acetylation crosstalk

Small-molecule TIP60 inhibitors enhance regulatory T cell induction through TIP60-P300 acetylation crosstalk

Interactions between Lipid Vesicle Membranes and Single Amino Acid Fibrils: Probable Origin of Specific Neurological Disorders

Single-Molecule Orientation Imaging Reveals the Nano-Architecture of Amyloid Fibrils Undergoing Growth and Decay

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