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Systematic investigations on the biophysical complexation of hydroxyethyl starch 200/0.5 with human serum albumin

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Abstract

Spectroscopic techniques have been used to improve the understanding of the interactions between hydroxyethyl starch (HES) 200/0.5 and human serum albumin (HSA) in a simulated physiological fluid of pH 7.4. It has been revealed that static fluorescence quenching occurred when HSA interacted with HES 200/0.5. The negative value of ΔH° (− 2.39 × 104 J·mol−1) and positive value of ΔS° (30.1 J·mol−1·K−1) suggested electrostatic interaction was the dominating force of the binding reaction between HES 200/0.5 to HSA, and the binding process was proved as a spontaneous one with negative ΔG° values (− 3.34 × 105 J·mol−1 at body temperature). The distance between HSA and HES 200/0.5 (r = 2.11 nm) proved efficient energy transfer from Trp to the drug. Moreover, the binding site of HES 200/0.5 to HSA was confirmed by site marker competitive experiments as Sudlow’s site I. Finally, it was observed that the conformation of HSA was changed with a loss of α-helical but acquisition of β contents, where a more stabilized secondary structure was formed.

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Acknowledgements

The authors thank the Medical and Health Technology Development Project of Shandong Province (No. 202013010367) and Yantai Technology and Innovation Development Scheme (No. 2021MSGY048) for financial support.

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JZ: Conceptualization, Methodology, Investigation, Writing—original draft. TW: Conceptualization, Methodology, Investigation, Writing—original draft. SH: Conceptualization, Methodology, Writing—review & editing. JL: Conceptualization, Writing—review & editing. HM: Conceptualization, Methodology, Investigation, Writing—original draft, Writing—review & editing.

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Correspondence to Huashan Ma.

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Zhang, J., Wang, T., Huang, S. et al. Systematic investigations on the biophysical complexation of hydroxyethyl starch 200/0.5 with human serum albumin. J Incl Phenom Macrocycl Chem 102, 743–750 (2022). https://doi.org/10.1007/s10847-022-01155-0

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