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2023•Nature BiotechnologyOpen access

Near-infrared co-illumination of fluorescent proteins reduces photobleaching and phototoxicity

Lucie Ludvíková, Emma Simon, Mathieu Deygas, Thomas Panier, Marie‐Aude Plamont, Jean Ollion, Alison G. Tebo, Matthieu Piel, Ludovic Jullien, Lydia Robert, Thomas Le Saux, Agathe Espagne

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Abstract

Here we present a method to reduce the photobleaching of fluorescent proteins and the associated phototoxicity. It exploits a photophysical process known as reverse intersystem crossing, which we induce by near-infrared co-illumination during fluorophore excitation. This dual illumination method reduces photobleaching effects 1.5-9.2-fold, can be easily implemented on commercial microscopes and is effective in eukaryotic and prokaryotic cells with a wide range of fluorescent proteins.

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Here we present a method to reduce the photobleaching of fluorescent proteins and the associated phototoxicity. It exploits a photophysical process known as reverse intersystem crossing, which we induce by near-infrared co-illumination during fluorophore excitation. This dual illumination method reduces photobleaching effects 1.5-9.2-fold, can be easily implemented on commercial microscopes and is effective in eukaryotic and prokaryotic cells with a wide range of fluorescent proteins.

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Available abstract

Here we present a method to reduce the photobleaching of fluorescent proteins and the associated phototoxicity. It exploits a photophysical process known as reverse intersystem crossing, which we induce by near-infrared co-illumination during fluorophore excitation. This dual illumination method reduces photobleaching effects 1.5-9.2-fold, can be easily implemented on commercial microscopes and is effective in eukaryotic and prokaryotic cells with a wide range of fluorescent proteins.

Key concepts: Photobleaching, Phototoxicity, Fluorophore, Fluorescence, Intersystem crossing, Chemistry, Biophysics, Photochemistry

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