Spectroscopic investigation of the interaction between human serum albumins and 10-hydroxycamptothecin |
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Authors: | Guizhi Li Yongming Liu |
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Affiliation: | (1) College of Chemistry, Yantai University, Yantai, 264005, Shandong, China |
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Abstract: | The binding reaction between 10-hydroxycamptothecin (10-HCPT) and human serum albumins (HSA) is studied by means of fluorescence spectroscopy, UV-Vis absorption spectrum, 1H NMR spectrum, and molecular simulation. The results indicate that the binding reaction of 10-HCPT and HSA is a single static quenching process, and the binding equilibrium constant for 10-HCPT binding with HSA is estimated K 0= 4.93×104 L · mol−1 at 25 °C with the molar ratio of 1:1. The distance (r) and energy transfer efficiency (E) between donor (HSA) and acceptor (10-HCPT) are obtained as follows, r =3.51 nm; E =0.27. The enthalpy change (ΔH ⦵) and entropy change (ΔS ⦵) are calculated at different temperatures, and the hydrophobic force and shidipole force are the functions in the reaction. The results show that 10-HCPT binds within the subdomain II A of HSA by the hydrophobic force, and the 10-OH and 20-OH of 10-HCPT bind with both residue Leu-238 of HSA and Ala 291 of HSA by hydrogen bonds. Biography: LI Guizhi(1962–), female, Associate professor, research direction: organic analysis. |
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Keywords: | 10-hydroxycamptothecin human serum albumins (HSA) fluorescence spectroscopy UV absorption spectroscopy 1H NMR spectrum molecular simulation |
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