BBS and NIR fluorescence
Free biliverdin has negligible fluorescence in solution. However, upon binding to biliverdin-binding serpins (BBSs), it emits light in the far-red and near-infrared regions of the spectrum.
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This emission falls within the optical window, a spectral region where light absorption and scattering by animal tissues are relatively low, allowing fluorescence to be detected in vivo, even from deep tissues.
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NIR-fluorescence emission of the glassfrog Teratohyla pulverata. Ex: 660 nm, Emission 745–755nm
While the biological significance of near-infrared (NIR) fluorescence—if any—remains unclear, NIR emission is a highly desirable feature of fluorescent probes used in biological and biomedical research because it enables imaging deeper within animal tissues.
In the lab, we are investigating dozens of newly discovered NIR-fluorescent biliproteins, using an evolutionary biochemistry framework to reconstruct the sequence of amino acid changes that shaped the evolution of their fluorescence, including changes in both emission intensity and wavelength.
In addition to evolutionary biochemistry approaches, we complement these studies with directed mutagenesis and rational protein design.
In the lab, we are investigating dozens of newly discovered NIR-fluorescent biliproteins, using an evolutionary biochemistry framework to reconstruct the sequence of amino acid changes that shaped the evolution of their fluorescence, including changes in both emission intensity and wavelength.
In addition to evolutionary biochemistry approaches, we complement these studies with directed mutagenesis and rational protein design.