Spectroscopic Evaluation of Novel TacrineCoumarin Hybrids as HSA-Interacting Agents

Abstract

In this work, we investigated the human serum albumin binding behavior of a series of novel derivatives with both tacrine and coumarin pharmacophores. The compounds were investigated using UV-Vis absorption and fluorescence spectroscopy. KB values were found to be in order of 103 M-1. The values of n indicate that only one independent class of binding sites is available for tacrine-coumarin hybrids on HSA. Synchronous fluorescence spectra showed that compounds did not have any noticeably effect on α-helical conformation of HSA. Our data indicated that these tacrine-coumarin molecules exhibit promising potential which would be of considerable use in the development of drugs with enhanced or more selective effects and greater clinical efficacy.