Investigation of new indole derivatives of bovine serum albumin using spectroscopic and molecular docking techniques

We investigated the interaction of two derivatives of bis (indolyl) methane with bovine serum albumin (BSA) using spectroscopic and molecular docking calculations. Fluorescence quenching measurements revealed that the quenching mechanism was static. F0rster energy transfer measurements, synchronous fluorescence spectroscopy and docking studies demonstrated that both bis(indolyl)methanes bound to the Trp residues of BSA. The docking study confirmed that both bis(indolyl)methanes form hydrogen bonds and van der Waals interactions with BSA. Our molecular docking study indicated that the compounds are located within the binding pocket of subdomains IIB and IB of BSA. Fourier transform infrared spectroscopy demonstrated that both bis(indolyl)methane derivatives can interact with BSA and can affect the secondary structure of BSA.