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

IF 2.3 4区 化学 Q2 Agricultural and Biological Sciences Journal of Inclusion Phenomena and Macrocyclic Chemistry Pub Date : 2022-07-22 DOI:10.1007/s10847-022-01155-0
Jianzhong Zhang, Tianyi Wang, Shaoyan Huang, Jie Li, Huashan Ma
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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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羟乙基淀粉200/0.5与人血清白蛋白生物物理络合的系统研究
在pH值为7.4的模拟生理液中,利用光谱技术研究了羟乙基淀粉(HES) 200/0.5与人血清白蛋白(HSA)之间的相互作用。结果表明,HSA与HES 200/0.5相互作用时发生静态荧光猝灭。负的ΔH°(−2.39 × 104 J·mol−1)和正的ΔS°(30.1 J·mol−1·K−1)表明,静电相互作用是HES 200/0.5与HSA结合反应的主导力,并且在体温下负的ΔG°(−3.34 × 105 J·mol−1)证明了结合过程是自发的。HSA与HES 200/0.5之间的距离(r = 2.11 nm)证明了Trp向药物的有效能量传递。此外,通过位点标记竞争实验证实了HES 200/0.5与HSA的结合位点为Sudlow位点i。最后,观察到HSA的构象发生了变化,α-螺旋结构丢失,β含量获得,形成了更稳定的二级结构。
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来源期刊
CiteScore
3.30
自引率
8.70%
发文量
0
审稿时长
3-8 weeks
期刊介绍: The Journal of Inclusion Phenomena and Macrocyclic Chemistry is the premier interdisciplinary publication reporting on original research into all aspects of host-guest systems. Examples of specific areas of interest are: the preparation and characterization of new hosts and new host-guest systems, especially those involving macrocyclic ligands; crystallographic, spectroscopic, thermodynamic and theoretical studies; applications in chromatography and inclusion polymerization; enzyme modelling; molecular recognition and catalysis by inclusion compounds; intercalates in biological and non-biological systems, cyclodextrin complexes and their applications in the agriculture, flavoring, food and pharmaceutical industries; synthesis, characterization and applications of zeolites. The journal publishes primarily reports of original research and preliminary communications, provided the latter represent a significant advance in the understanding of inclusion science. Critical reviews dealing with recent advances in the field are a periodic feature of the journal.
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