Jianzhong Zhang, Tianyi Wang, Shaoyan Huang, Jie Li, Huashan Ma
{"title":"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","authors":"Jianzhong Zhang, Tianyi Wang, Shaoyan Huang, Jie Li, Huashan Ma","doi":"10.1007/s10847-022-01155-0","DOIUrl":null,"url":null,"abstract":"<div><p>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 Δ<i>H</i>° (− 2.39 × 10<sup>4</sup> J·mol<sup>−1</sup>) and positive value of Δ<i>S</i>° (30.1 J·mol<sup>−1</sup>·K<sup>−1</sup>) 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 Δ<i>G</i>° values (− 3.34 × 10<sup>5</sup> J·mol<sup>−1</sup> at body temperature). The distance between HSA and HES 200/0.5 (<i>r</i> = 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.</p></div>","PeriodicalId":638,"journal":{"name":"Journal of Inclusion Phenomena and Macrocyclic Chemistry","volume":"102 9-10","pages":"743 - 750"},"PeriodicalIF":2.3000,"publicationDate":"2022-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Systematic investigations on the biophysical complexation of hydroxyethyl starch 200/0.5 with human serum albumin\",\"authors\":\"Jianzhong Zhang, Tianyi Wang, Shaoyan Huang, Jie Li, Huashan Ma\",\"doi\":\"10.1007/s10847-022-01155-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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 Δ<i>H</i>° (− 2.39 × 10<sup>4</sup> J·mol<sup>−1</sup>) and positive value of Δ<i>S</i>° (30.1 J·mol<sup>−1</sup>·K<sup>−1</sup>) 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 Δ<i>G</i>° values (− 3.34 × 10<sup>5</sup> J·mol<sup>−1</sup> at body temperature). The distance between HSA and HES 200/0.5 (<i>r</i> = 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.</p></div>\",\"PeriodicalId\":638,\"journal\":{\"name\":\"Journal of Inclusion Phenomena and Macrocyclic Chemistry\",\"volume\":\"102 9-10\",\"pages\":\"743 - 750\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2022-07-22\",\"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/s10847-022-01155-0\",\"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/s10847-022-01155-0","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}
Systematic investigations on the biophysical complexation of hydroxyethyl starch 200/0.5 with human serum albumin
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.
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.