Spectroscopic Insights of an Emissive Complex between 4'-N,N-Diethylaminoflavonol in Octa-Acid Deep-Cavity Cavitand and Rhodamine 6G.

Excited-state chemistry relies on the communication between molecules, making it a crucial aspect of the field. One important question that arises is whether intermolecular communication and its rate can be modified when a molecule is confined. To explore the interaction in such systems, we investigated the ground and excited states of 4'-N,N-diethylaminoflavonol (DEA3HF) in an octa acid-based (OA) confined medium and in ethanolic solution, both in the presence of Rhodamine 6G (R6G). Despite the observed spectral overlap between the flavonol emission and the R6G absorption, as well as the fluorescence quenching of the flavonol in the presence of R6G, the almost constant fluorescence lifetime at different amounts of R6G discards the presence of FRET in the studied systems. Steady-state and time-resolved fluorescence indicate the formation of an emissive complex between the proton transfer dye encapsulated within water-soluble supramolecular host octa acid (DEA3HF@(OA)2) and R6G. A similar result was observed between DEA3HF:R6G in ethanolic solution. The respective Stern-Volmer plots corroborate with these observations, suggesting a static quenching mechanism for both systems.

Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA.

In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emission with a large Stokes shift in the blue-green regions due to a proton transfer process in the excited state. The interactions of the benzazoles with BSA were studied using UV-Vis absorption and steady-state fluorescence spectroscopy. The observed spectral quenching of BSA indicates that these compounds could bind to BSA through a strong binding affinity afforded by a static quenching mechanism (Kq~1012 L·mol-1·s-1). The docking simulations indicate that compounds 13 and 16 bind closely to Trp134 in domain I, adopting similar binding poses and interactions. On the other hand, compounds 12, 14, 15, and 17 were bound between domains I and III and did not directly interact with Trp134.