Abstract
The interactions between myriocin (ISP-1) and human serum albumin (HSA) were studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach. The intrinsic fluorescence of HSA was quenched through a combination of static and dynamic quenching. The binding constants and the number of binding sites were evaluated according to the Stern–Volmer equation. ISP-1 could not bind efficiently to HSA at higher temperatures. The electrostatic force, hydrogen bonding and hydrophobic force were dominant for the binding ISP-1 and HSA. The site I was the primary binding site for the binding ISP-1 and HSA. What’s more, the conformational and microenvironmental changes of HSA during the binding process were studied by synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. Lys-195, Arg-218, Arg-222 and Val-293 were the important amino acid residues involved in the binding process.
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