Spectroscopic and molecular modeling investigation on the binding of a synthesized steroidal amide to protein

摘要: Abstract Owing to the various valuable biological activities, steroidal amides have become a hot topic in pharmaceutical chemistry. In this paper, an anti-tumor steroid derivate (DAAO) was synthesized and identified. The interaction between DAAO human serum albumin (HSA) studied by fluorescence spectra, circular dichroism (CD) molecular modeling probe techniques. results suggested that had reacted with HSA through hydrogen bonds van der Waals power. formation of DAAO–HSA complex at ground state led static quenching HSA׳s fluorescence. number binding sites, constants, enthalpy change (Δ H θ ), Gibbs free energy G ) entropy S were calculated different temperatures based on theory classic equation. Molecular investigation indicated more inclined absorb Sudlow׳s site I subdomain IIA molecule grounds lowest principle steric hindrance effect. location further confirmed experiment using warfarin (site probe) for displacement. Furthermore, conformational changes presence investigated CD spectra. could provide new evidence explaining relationship chemical structure activity may be useful understanding anti-cancer mechanism drug.