Investigations of interaction mechanism and conformational variation of serum albumin affected by artemisinin and dihydroartemisinin

IF 2.3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY Journal of Molecular Recognition Pub Date : 2022-10-31 DOI:10.1002/jmr.3000
Rukui Zhu, Yu Liang, Huajian Luo, Huishan Cao, Yi Liu, Shan Huang, Qi Xiao
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引用次数: 1

Abstract

In this work, binding interactions of artemisinin (ART) and dihydroartemisinin (DHA) with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated thoroughly to illustrate the conformational variation of serum albumin. Experimental results indicated that ART and DHA bound strongly with the site I of serum albumins via hydrogen bond (H-bond) and van der Waals force and subsequently statically quenched the intrinsic fluorescence of serum albumins through concentration-dependent manner. The quenching abilities of two drugs on the intrinsic fluorescence of HSA were much higher than the quenching abilities of two drugs on the intrinsic fluorescence of BSA. Both ART and DHA, especially DHA, caused the conformational variation of serum albumins and reduced the α-helix structure content of serum albumins. DHA with hydrophilic hydroxyl group bound with HSA more strongly, suggesting the important roles of the chemical polarity and the hydrophilicity during the binding interactions of two drugs with serum albumins. These results reveal the molecular understanding of binding interactions between ART derivatives and serum albumins, providing vital information for the future application of ART derivatives in biological and clinical areas.

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青蒿素与双氢青蒿素对血清白蛋白相互作用机制及构象变化的影响
本工作深入研究了青蒿素(ART)和双氢青蒿素(DHA)与人血清白蛋白(HSA)和牛血清白蛋白(BSA)的结合相互作用,以阐明血清白蛋白的构象变化。实验结果表明,ART和DHA通过氢键(H-bond)和范德华力与血清白蛋白位点I强结合,随后通过浓度依赖性方式静态猝灭血清白蛋白的固有荧光。两种药物对HSA本征荧光的猝灭能力远高于两种药物对牛血清白蛋白本征荧光猝灭能力。ART和DHA,尤其是DHA,都引起血清白蛋白的构象变化,降低血清白蛋白的α-螺旋结构含量。具有亲水性羟基的DHA与HSA的结合更强,表明化学极性和亲水性在两种药物与血清白蛋白的结合过程中发挥着重要作用。这些结果揭示了对ART衍生物与血清白蛋白之间结合相互作用的分子理解,为ART衍生物在生物学和临床领域的未来应用提供了重要信息。
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来源期刊
Journal of Molecular Recognition
Journal of Molecular Recognition 生物-生化与分子生物学
CiteScore
4.60
自引率
3.70%
发文量
68
审稿时长
2.7 months
期刊介绍: Journal of Molecular Recognition (JMR) publishes original research papers and reviews describing substantial advances in our understanding of molecular recognition phenomena in life sciences, covering all aspects from biochemistry, molecular biology, medicine, and biophysics. The research may employ experimental, theoretical and/or computational approaches. The focus of the journal is on recognition phenomena involving biomolecules and their biological / biochemical partners rather than on the recognition of metal ions or inorganic compounds. Molecular recognition involves non-covalent specific interactions between two or more biological molecules, molecular aggregates, cellular modules or organelles, as exemplified by receptor-ligand, antigen-antibody, nucleic acid-protein, sugar-lectin, to mention just a few of the possible interactions. The journal invites manuscripts that aim to achieve a complete description of molecular recognition mechanisms between well-characterized biomolecules in terms of structure, dynamics and biological activity. Such studies may help the future development of new drugs and vaccines, although the experimental testing of new drugs and vaccines falls outside the scope of the journal. Manuscripts that describe the application of standard approaches and techniques to design or model new molecular entities or to describe interactions between biomolecules, but do not provide new insights into molecular recognition processes will not be considered. Similarly, manuscripts involving biomolecules uncharacterized at the sequence level (e.g. calf thymus DNA) will not be considered.
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