Fret Atp Probe
Fret Atp Probe - Related Videos
03:40
Imaging Intracellular ATP Dynamics Using FRET-Based Sensors in an Organotypic Mouse Hippocampal Slice
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2025
Source: Lerchundi, R., et. al. Imaging of Intracellular ATP in Organotypic Tissue Slices of the Mouse Brain using the FRET-based Sensor ATeam1.03YEMK. J. Vis. Exp. (2019)This video demonstrates the use of FRET(Fluorescence Resonance Energy Transfer)-based sensors to measure intracellular ATP levels in organotypic mouse hippocampal slices, enabling real-time visualization of ATP dynamics in neurons and astrocytes under physiological and experimental conditions.
01:31
ATP Yield
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2019
Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle). The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...
09:47
FRET Imaging in Three-dimensional Hydrogels
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Cited by 3 •
2016
Förster resonance energy transfer (FRET) imaging is a powerful tool for real-time cell biology studies. Here a method for FRET imaging cells in physiologic three-dimensional (3D) hydrogel microenvironments using conventional epifluorescence microscopy is presented. An analysis for ratiometric FRET probes that yields linear ratios over the activation range is described.
08:32
The ATP Bioluminescence Assay
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2023
In fireflies, the luciferase enzyme converts a compound called luciferin into oxyluciferin, and produces light or “luminescence” as a result. This reaction requires energy derived from ATP in order to proceed, so researchers have exploited the luciferase-luciferin interaction to gauge ATP levels in cells. Given ATP’s role as the cell’s currency of energy, the ATP bioluminescence assay can provide insight into cellular metabolism and overall cell health.In this video, JoVE discusses cellular...
01:08
Hydrolysis of ATP
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2019
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids. If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
FAQs
The ATP-binding domain serves as the recognition component, while the donor and acceptor fluorophores report structural changes. When ATP binds, the domain can change the probe’s conformation or alter the distance between fluorophores. That physical change modifies Förster resonance energy transfer, allowing the binding event to appear as a measurable change in fluorescence.
The fluorescence ratio links the donor and acceptor signals to the probe’s ATP-responsive state. Using this ratio provides an optical readout of ATP-related changes rather than relying on a single fluorescence channel alone. In living cells or engineered systems, the resulting measurement can be compared across conditions to assess changes in energy state.
Spatial resolution shows where ATP-related differences occur within a living cell, engineered system, or biomaterial, while temporal resolution shows how those differences change over time. Together, these dimensions can reveal localized or condition-dependent energy behavior that a single measurement of overall ATP levels might not distinguish.
The probe converts ATP recognition into a fluorescence response, so changes in ATP availability can produce corresponding changes in the measured signal. Comparing readings across conditions or after an intervention helps associate altered fluorescence ratios with shifts in energy state. This makes the probe useful for examining how biological systems respond to changing circumstances.
A study places the probe in a living cell or engineered biological system, records the donor and acceptor fluorescence, and evaluates the resulting fluorescence ratio. Measurements can then be collected under different conditions or after an intervention. Comparing those readings helps determine whether ATP availability changes and where or when the response occurs.
In engineered cells, the probe can reveal how ATP availability changes as cellular designs or metabolic pathways are evaluated. Researchers can monitor energy-state responses across conditions rather than examining pathway performance without an ATP readout. This information supports assessment of whether an engineered configuration maintains or alters ATP availability within the biological system.
FRET ATP probes extend ATP monitoring beyond cells to engineered biological systems and biomaterials. Their optical readout can show how ATP availability varies across conditions or responds to interventions in these designed environments. Such measurements provide bioengineering context for evaluating energy-related behavior while preserving information about spatial and temporal changes.