{"title":"利用多重光谱探究环丙氟哌酸与人血清白蛋白的相互作用","authors":"Qiao Pan, Chengfeng Yao, Yulin Zhu, Shujun Shang","doi":"10.1007/s10847-024-01241-5","DOIUrl":null,"url":null,"abstract":"<div><p>The interaction between ciprofol and human serum albumin (HSA) was studied using spectroscopy-based approaches at different temperatures under simulated physiological conditions <i>in vitro</i>. Quenching of intrinsic Trp fluorescence of HSA with increasing ciprofol concentration is the actuating tool in the analysis. Experimental results proved that ciprofol quenched the intrinsic fluorescence of HSA through a static quenching mechanism. The thermodynamic parameters (Δ<i>G</i> = -2.35 × 10<sup>4</sup> J·mol<sup>−1</sup>, Δ<i>S</i> = -131 J·mol<sup>−1</sup>·K<sup>−1</sup>, and Δ<i>H</i> = -6.39 × 10<sup>4</sup> J·mol<sup>−1</sup> at 310 K), binding sites (<i>n</i> = 0.83), and binding constant (<i>K</i><sub>A</sub> = 9.12 × 10<sup>3</sup> M<sup>−1</sup>) indicated that hydrogen bond and van der Waals forces played a major role in the HSA-ciprofol association with weak binding force. Furthermore, the circular dichroism, synchronous, and three-dimensional fluorescence spectral results indicated adaptive structural changes of HSA in the presence of ciprofol. In addition, the effect of some common metal ions on the binding between ciprofol and HSA was examined, and Fe<sup>3+</sup> and Hg<sup>2+</sup> were proven to help prolong the storage time and improve the drug efficacy. The study provides accurate and full basic data for clarifying the binding mechanisms of ciprofol with HSA and helps understand its effect on protein function during the blood transportation process and activity in vivo.</p></div>","PeriodicalId":638,"journal":{"name":"Journal of Inclusion Phenomena and Macrocyclic Chemistry","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Probing the interaction of ciprofol and human serum albumin using multiple spectroscopies\",\"authors\":\"Qiao Pan, Chengfeng Yao, Yulin Zhu, Shujun Shang\",\"doi\":\"10.1007/s10847-024-01241-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The interaction between ciprofol and human serum albumin (HSA) was studied using spectroscopy-based approaches at different temperatures under simulated physiological conditions <i>in vitro</i>. Quenching of intrinsic Trp fluorescence of HSA with increasing ciprofol concentration is the actuating tool in the analysis. Experimental results proved that ciprofol quenched the intrinsic fluorescence of HSA through a static quenching mechanism. The thermodynamic parameters (Δ<i>G</i> = -2.35 × 10<sup>4</sup> J·mol<sup>−1</sup>, Δ<i>S</i> = -131 J·mol<sup>−1</sup>·K<sup>−1</sup>, and Δ<i>H</i> = -6.39 × 10<sup>4</sup> J·mol<sup>−1</sup> at 310 K), binding sites (<i>n</i> = 0.83), and binding constant (<i>K</i><sub>A</sub> = 9.12 × 10<sup>3</sup> M<sup>−1</sup>) indicated that hydrogen bond and van der Waals forces played a major role in the HSA-ciprofol association with weak binding force. Furthermore, the circular dichroism, synchronous, and three-dimensional fluorescence spectral results indicated adaptive structural changes of HSA in the presence of ciprofol. In addition, the effect of some common metal ions on the binding between ciprofol and HSA was examined, and Fe<sup>3+</sup> and Hg<sup>2+</sup> were proven to help prolong the storage time and improve the drug efficacy. The study provides accurate and full basic data for clarifying the binding mechanisms of ciprofol with HSA and helps understand its effect on protein function during the blood transportation process and activity in vivo.</p></div>\",\"PeriodicalId\":638,\"journal\":{\"name\":\"Journal of Inclusion Phenomena and Macrocyclic Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-04-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Inclusion Phenomena and Macrocyclic Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s10847-024-01241-5\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"Agricultural and Biological Sciences\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Inclusion Phenomena and Macrocyclic Chemistry","FirstCategoryId":"92","ListUrlMain":"https://link.springer.com/article/10.1007/s10847-024-01241-5","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
Probing the interaction of ciprofol and human serum albumin using multiple spectroscopies
The interaction between ciprofol and human serum albumin (HSA) was studied using spectroscopy-based approaches at different temperatures under simulated physiological conditions in vitro. Quenching of intrinsic Trp fluorescence of HSA with increasing ciprofol concentration is the actuating tool in the analysis. Experimental results proved that ciprofol quenched the intrinsic fluorescence of HSA through a static quenching mechanism. The thermodynamic parameters (ΔG = -2.35 × 104 J·mol−1, ΔS = -131 J·mol−1·K−1, and ΔH = -6.39 × 104 J·mol−1 at 310 K), binding sites (n = 0.83), and binding constant (KA = 9.12 × 103 M−1) indicated that hydrogen bond and van der Waals forces played a major role in the HSA-ciprofol association with weak binding force. Furthermore, the circular dichroism, synchronous, and three-dimensional fluorescence spectral results indicated adaptive structural changes of HSA in the presence of ciprofol. In addition, the effect of some common metal ions on the binding between ciprofol and HSA was examined, and Fe3+ and Hg2+ were proven to help prolong the storage time and improve the drug efficacy. The study provides accurate and full basic data for clarifying the binding mechanisms of ciprofol with HSA and helps understand its effect on protein function during the blood transportation process and activity in vivo.
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.