RSC Advances · 2018 · 98 citations · 34 references
PharmacyBiochemistryPharmacologyBiophysical ChemistrySpectroscopyStructure-activity RelationshipsFluorescence SpectroscopyLigand BindingMolecular DockingProtein BindingProtein ChemistryProtein-ligand DockingBovine Serum AlbuminEquilibrium Binding ConstantFluorescence QuenchingHydrogen BondingIntrinsic FluorescenceMolecular Docking AnalysisProtein Conformational ChangesTraditional Chinese Medicine
≈ 1) at 298 K suggested that ASN only occupied one site in BSA with high affinity. Moreover, the results of molecular docking indicated that ASN was more likely to be located in site I (sub-domain IIA) of BSA. The results of synchronous fluorescence and three-dimensional fluorescence spectra showed that ASN induced conformational changes of BSA. The findings would be beneficial for research on the transportation, distribution and some important bioactivities of ASN in the human body.
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