羟乙基淀粉 130/0.4 负载白蛋白纳米粒子的合成:生物相容性和相互作用机制

IF 2.3 4区 化学 Q2 Agricultural and Biological Sciences Journal of Inclusion Phenomena and Macrocyclic Chemistry Pub Date : 2024-01-02 DOI:10.1007/s10847-023-01217-x
Heng Wang, Shaoyan Huang, Jianzhong Zhang, Jie Li, Mingming Liu
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摘要

纳米药物平台在血液中具有良好的稳定性和较高的治疗优势。在此,我们利用羟乙基淀粉(HES)130/0.4 和血清白蛋白这两种在静脉治疗中广泛使用的容量扩张剂,合成了一种新型的 HES 130/0.4 负载牛血清白蛋白(BSA)纳米颗粒,并在考虑相容性的前提下研究了其在模拟生理环境中的结合机制。利用 Stern-Volmer 方程分析了 HES 对 BSA 的荧光淬灭数据,证明形成了 1:1 的基态复合物。体温下的结合参数(ΔS° = 329 J mol-1 K-1,ΔH° = 6.38 × 105 J mol-1,ΔG = - 3.04 × 105 J mol-1)表明,这种相互作用是放热的,由疏水相互作用驱动。计算得出的结合距离为 2.73 nm,表明佛斯特共振能量转移的可能性很高。通过应用三维/同步荧光和圆二色性技术,分别对 BSA 的结构变化进行了定性和定量评估,结果显示二级结构发生了适应性变化。本研究的结果不仅为基于白蛋白的 NP 合成提供了新思路,而且提供了精确、全面的原始数据,阐明了 HES 与 BSA 的相互作用机制,有助于理解其在血液中的药效学。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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The synthesis of hydroxyethyl starch 130/0.4-loaded albumin nanoparticles: biocompatibility and interaction mechanism

The nanoplatform for drugs demonstrates favorable stability and high therapeutical advantages in the bloodstream. Here, by using hydroxyethyl starch (HES) 130/0.4 and serum albumin, which were widely used as volume expanders in intravenous therapy, we synthesized a new HES 130/0.4-loaded bovine serum albumin (BSA) nanoparticles and investigated the binding mechanism in the simulated physiological environment with considerations of compatibility. Analysis of the fluorescence quenching data of BSA by HES using the Stern–Volmer equation proved the formation of a 1:1 ground state complex. The binding parameters (ΔS° = 329 J mol−1 K−1, ΔH° = 6.38 × 105 J mol−1, and ΔG = − 3.04 × 105 J mol−1) at body temperature manifested that the interaction was exothermic and driven by hydrophobic interactions. The binding distance was calculated as 2.73 nm and showed a high possibility of Förster resonance energy transfer. The structural alterations of BSA were assessed both qualitatively and quantitatively through the application of 3D/synchronous fluorescence and circular dichroism techniques, respectively, which showed adaptive changes in secondary structures. The results presented in this study offer not only novel ideas of albumin-based NP synthesis, but precise and comprehensive primary data that elucidate the mechanisms of HES-BSA interaction, helping to comprehend its pharmacodynamics in blood.

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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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