Subnanosecond spectrofluorimetry of new indolocarbazole derivatives in solutions and protein complexes and their dipole moments |
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Authors: | N?A?Nemkovich Yu?V?Kruchenok A?N?Sobchuk H?Detert N?Wrobel E?A?Chernyavski? |
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Institution: | (1) Department of Chemistry, Illinois State University, Normal, IL 61790-4160, USA |
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Abstract: | The spectral and temporal characteristics of new 6,12-dimethoxyindolo3,2-b]carbazole, 5,11-dimethyl-6,12-dimethoxyindolo3,2-b]carbazole, and 5,11-dihexyl-6,12-di(hexyloxy)indolo3,2-b]carbazole fluorescence probes in organic solvents and protein complexes are studied. The dipole moments of indolocarbazoles
in 1,4-dioxane were measured by electrooptical absorption method. The measured dipole moments have values within the range
of (3.1–3.6) × 10−30 C m in the equilibrium ground state and increase to (4.8–5.6) × 10−30 C m after excitation. The excited state lifetime of indolocarbazole derivatives increases with increasing polarity and viscosity
of the environment. The binding of indolocarbazoles with trypsinogen and human serum albumin increases the fluorescence intensity,
changes the intensity ratio of fluorescence bands, and increases the average excited state lifetime of indolocarbazoles. The
analysis of the instantaneous fluorescence spectra and fluorescence decay parameters at different wavelengths revealed the
existence of several types of probe binding sites in proteins. It is found that the fluorescence characteristics of indolocarbazole
derivatives depend on the conformation rearrangements of trypsinogen due to its thermal denaturation. |
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