Nahid Shahabadi - Faculty of Chemistry, Razi University, Kermanshah, ۶۷۱۴۹, Iran, Medical Biology Research Center (MBRC), University of Medical Sciences, Kermanshah, Iran
mahtab razlanasri - Institute of Nano Science and Nano Technology, Razi University, Kermanshah, ۶۷۱۴۹, Iran

In the present work, the interaction of Fe3O4@CaAl LDH@ Lamivudine with human serum albumin (HSA) was investigated by applying UV–vis and fluorescence spectra. The nanocomposite was quenching the natural fluorescence of HSA, which was indicated the static quenching mechanism. The consequences demonstrated that this nanocomposite can strongly bind to HSA molecules. According to fluorescence quenching computations, the bimolecular quenching constant (kq), apparent quenching constant (KSV) at various temperatures were calculated (288, 298, 310 k). The binding constants Kb were 12187.09 L mol−1, 62849.24 L mol−1 and 350429 L mol−1 at 288 K, 298 K and 310 K respectively, and the number of binding sites n is almost > 1. competitive results show that the binding site of nanocomposite placed in subdomain ІІІA (site ІІ) of HSA. The thermodynamic parameters defined by the Van’t Hoff analysis of the binding constants (ΔH 113.211 kJ mol−1 and ΔS 471.4703 J mol−1 K−1) clearly illustrated that the hydrophobic force plays a major role in the process. To compare binding behavior and mechanism of the antiviral drug which was loaded on Fe3O4@CaAl LDH with human serum albumin (HSA), we carried out fluorescence and UV-Visible spectroscopy to investigate the interactions of Fe3O4@CaAl LDH@ Lamivudine with HSA.

amivudine, nanocomposite, interaction, HSA