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- W2348399308 abstract "With the help of multitude spectroscopic techniques,such as fluorescence spectra and circular dichroism,the interaction between neferinr(NF)and human serum albumin(HSA)was studied.Experimental datas were dealed with Stern-Volmer plot and Line weaver-Burk equation.The NF has a powerful ability to quench the albumin's fluorescence in a static mode and the main binding forces were hydrophobic interaction and electrostatic action.Under 309K,the binding constant was 1.39×104L·mol-1.Distance between NF and tryptophan residue was 2.70nm.Thermodynamic parameters were ΔH0=-13.0kJ·mol-1,ΔS0=37.2J·(K·mol)-1.Binding of NF with HSA can increase the percentage of α-helix of HSA.There was little effect of bioactive components in traditional Chinese medicine(glycyrrhetinic acid etc)and fatty acids on the binding." @default.
- W2348399308 created "2016-06-24" @default.
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- W2348399308 date "2010-01-01" @default.
- W2348399308 modified "2023-09-25" @default.
- W2348399308 title "Study on the Interaction of Neferine with Human Serum Albumin" @default.
- W2348399308 hasPublicationYear "2010" @default.
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