NADH Fluorescence Properties Under Varying Temperature, pH, and Binding Conditions

Reduced nicotinamide adenine dinucleotide (NADH) is a key biomarker for probing metabolic state. Imperial College London researcher Taylor M. Cannon characterized its fluorescence intensity, lifetime, spectral response, anisotropy, and time-resolved anisotropy in aqueous solution using single-photon excitation at 375 nm. The data demonstrates how temperature, pH, and binding partners impact the fluorescence signature of NADH.

Use Cases

• Calibrating NADH fluorescence measurements based on temperature effects described in the study.
• Modeling the impact of pH on NADH fluorescence lifetime for in vivo metabolic sensing.
• Analyzing fluorescence anisotropy changes based on NADH binding to different partners.
• Benchmarking experimental setups against reference data for single-photon excitation at 375 nm.

Strengths

• Data originates from a controlled, cuvette-based time-resolved spectrofluorimeter setup.
• Characterizes multiple fluorescence properties: intensity, lifetime, spectral response, anisotropy, and time-resolved anisotropy.
• Systematically varies three key microenvironmental conditions: temperature, pH, and binding partners.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Imperial College London

Collection Method

Experimental measurements using a cuvette-based time-resolved spectrofluorimeter.