Analysis of the interaction of a new series of rhodanine derivatives with bovine serum albumin by fluorescence quenching

Abstract

The interaction between a series of rhodanine derivatives with different substituent groups and bovine serum albumin (BSA) was studied using fluorescence quenching spectra, which showed that the type of quenching of BSA by rhodanine derivatives was static in each case. Binding constants, binding site numbers, action distances, and energy transfer efficiencies between donor (BSA) and acceptors (rhodanine derivatives) were calculated and showed that introduction of –NO₂ (electron-withdrawing group) is more favorable for rhodanine–BSA interaction than that of –CH₃ and –OCH₃ (electron-donating groups). Finally, strength of interaction between rhodanine derivatives and BSA was simulated theoretically using quantum chemistry and showed that introduction of groups with small steric hindrance is beneficial to promote the interaction. These investigations are very important to simulate the interaction of small molecules with biomacromolecules and to synthesize drug molecules that interact with protein easily.

Graphical abstract