Subnanosecond spectrofluorimetry of new indolocarbazole derivatives in solutions and protein complexes and their dipole moments

• Published in: Optics and spectroscopy 2009-08, Vol.107 (2), p.275-281
• Main Authors: Nemkovich, N. A., Kruchenok, Yu. V., Sobchuk, A. N., Detert, H., Wrobel, N., Chernyavskiĭ, E. A.
• Format: Article
• Language: English
• Subjects: Condensed-Matter Spectroscopy; Lasers; Optical Devices; Optics; Photonics; Physics; Physics and Astronomy
• ISSN: 0030-400X; 1562-6911
• DOI: 10.1134/S0030400X09080189

The spectral and temporal characteristics of new 6,12-dimethoxyindolo[3,2- b ]carbazole, 5,11-dimethyl-6,12-dimethoxyindolo[3,2- b ]carbazole, and 5,11-dihexyl-6,12-di(hexyloxy)indolo[3,2- 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.