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Excited-State Proton Transfer Can Tune the Color of Protein Fluorescent Markers

Abstract : We show by quantum mechanical/molecular mechanical (QM/MM) simulations that phenylbenzothiazoles undergoing an excited-state proton transfer (ESPT) can be used to probe protein binding sites. For 2-(2'-hydroxy-4'-aminophenyl)benzothiazole (HABT) bound to a tyrosine kinase, the absolute and relative intensities of the fluorescence bands arising from the enol and keto forms are found to be strongly dependent on the active-site conformation. The emission properties are tuned by hydrogen-bonding interactions of HABT with the neighboring amino acid T766 and with active-site water. The use of ESPT tuners opens the possibility of creating two-color fluorescent markers for protein binding sites, with potential applications in the detection of mutations in cancer cell lines.
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https://hal-amu.archives-ouvertes.fr/hal-01415155
Contributor : Didier Siri <>
Submitted on : Monday, December 12, 2016 - 6:49:10 PM
Last modification on : Wednesday, November 6, 2019 - 9:16:02 AM

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Daiana T. Mancini, Kakali Sen, Mario Barbatti, Walter Thiel, Teodorico C. Ramalho. Excited-State Proton Transfer Can Tune the Color of Protein Fluorescent Markers. ChemPhysChem, Wiley-VCH Verlag, 2015, 16 (16), pp.3444--3449. ⟨10.1002/cphc.201500744⟩. ⟨hal-01415155⟩

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