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The development of a fluorescent LCK inhibitor that exhibits favourable solvatochromic properties upon binding the kinase enzyme is described. Fluorescent properties were realised through the inclusion of a Prodan-derived fluorophore into the pharmacophore of the ATP-competitive kinase inhibitor. Fluorescence titration experiments exemplify the solvatochromic properties of the inhibitor, in which dramatic increase in emission intensity and hypsochromic shift in emission maxima are clearly observed upon binding LCK. Microscopy experiments in cellular contexts together with flow cytometry show that the fluorescence intensity of the inhibitor correlates with the LCK concentration. Furthermore, multiphoton microscopy experiments demonstrate both the rapid cellular uptake of the inhibitor and that the two-photon cross section of the inhibitor is amenable for excitation at 700 nm.
This article was published in the following journal.
Name: Angewandte Chemie (International ed. in English)
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