Investigation on the protein-binding properties of icotinib by spectroscopic and molecular modeling method.

摘要: Icotinib is a highly-selective epidermal growth factor receptor tyrosine kinase inhibitor with preclinical and clinical activity in non-small cell lung cancer, which has been developed as new targeted anti-tumor drug China. In this work, the interaction of icotinib human serum albumin (HSA) were studied by three-dimensional fluorescence spectra, ultraviolet circular dichroism (CD) molecular probe modeling methods. The results showed that binds to Sudlow's site I subdomain IIA HSA molecule, resulting icotinib-HSA complexes formed at ground state. number binding sites, equilibrium constants, thermodynamic parameters reaction calculated different temperatures. negative enthalpy change (ΔH(θ)) entropy (ΔS(θ)) indicated structure was stabilized hydrogen bonds van der Waals power. distance between donor acceptor according Forster's non-radiation resonance energy transfer theory. structural changes caused detected synchronous spectra spectra. Molecular method employed unfold full details level, most could be supported experimental results. study analyzed probability albumins act carriers for anticarcinogen provided fundamental information on process delivering its target tissues, might helpful understanding mechanism cancer therapy.