Cibacron Blue F3GA与人血清白蛋白配合物的等温滴定量热结合特性

IF 2.3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Cenk A. Andac, Sena Çağlar, Adil Denizli, Müge Andaç
{"title":"Cibacron Blue F3GA与人血清白蛋白配合物的等温滴定量热结合特性","authors":"Cenk A. Andac,&nbsp;Sena Çağlar,&nbsp;Adil Denizli,&nbsp;Müge Andaç","doi":"10.1002/jmr.3040","DOIUrl":null,"url":null,"abstract":"<p>Binding interactions between Cibacron Blue-F3GA (CB-F3GA) and human serum albumin (HSA, at physiologically ten-fold lower concentration) was studied by isothermal titration calorimetry (ITC) and <i>in-silico</i> docking computations. ITC experiments revealed two separate binding sites on HSA with different binding affinities for CB-F3GA. The high-affinity binding site (PBS-II) on HSA binds CB-F3GA at nanomolar scale (K<sub>D1</sub> = 118 ± 107 nM) with favorable binding enthalpy (ΔH<sup>o</sup><sub>1</sub> = − 6.47 ± 0.44 kcal/mol) and entropy (−TΔS<sup>o</sup><sub>1</sub> = −2.98 kcal/mol) energies. CB-F3GA binds to the low-affinity binding site (PBS-I) at μM scale (K<sub>D2</sub> = 31.20 ± 18.40 μM) with favorable binding enthalpy (ΔH<sup>o</sup><sub>1</sub> = − 5.03 ± 3.86 × 10<sup>−2</sup> kcal/mol) and entropy (−TΔS<sup>o</sup><sub>1</sub> = −1.12 kcal/mol) energies. ITC binding data strongly suggest that CB-F3GA binding to PBS-II site increases the formation of dimeric-HSA clusters (N<sub>1</sub> = 2.43 ± 0.50), while binding to PBS-I leads to tetrameric-HSA clusters (N<sub>2</sub> = 4.61 ± 0.90). These results suggest that a higher degree of HSA aggregation upon drug binding may be expected under physiological conditions, a notion that should be further investigated for the delivery and toxicity of drug−HSA interactions.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"36 8","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2023-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Isothermal titration calorimetry binding properties of Cibacron Blue F3GA in complex with human serum albumin\",\"authors\":\"Cenk A. Andac,&nbsp;Sena Çağlar,&nbsp;Adil Denizli,&nbsp;Müge Andaç\",\"doi\":\"10.1002/jmr.3040\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Binding interactions between Cibacron Blue-F3GA (CB-F3GA) and human serum albumin (HSA, at physiologically ten-fold lower concentration) was studied by isothermal titration calorimetry (ITC) and <i>in-silico</i> docking computations. ITC experiments revealed two separate binding sites on HSA with different binding affinities for CB-F3GA. The high-affinity binding site (PBS-II) on HSA binds CB-F3GA at nanomolar scale (K<sub>D1</sub> = 118 ± 107 nM) with favorable binding enthalpy (ΔH<sup>o</sup><sub>1</sub> = − 6.47 ± 0.44 kcal/mol) and entropy (−TΔS<sup>o</sup><sub>1</sub> = −2.98 kcal/mol) energies. CB-F3GA binds to the low-affinity binding site (PBS-I) at μM scale (K<sub>D2</sub> = 31.20 ± 18.40 μM) with favorable binding enthalpy (ΔH<sup>o</sup><sub>1</sub> = − 5.03 ± 3.86 × 10<sup>−2</sup> kcal/mol) and entropy (−TΔS<sup>o</sup><sub>1</sub> = −1.12 kcal/mol) energies. ITC binding data strongly suggest that CB-F3GA binding to PBS-II site increases the formation of dimeric-HSA clusters (N<sub>1</sub> = 2.43 ± 0.50), while binding to PBS-I leads to tetrameric-HSA clusters (N<sub>2</sub> = 4.61 ± 0.90). These results suggest that a higher degree of HSA aggregation upon drug binding may be expected under physiological conditions, a notion that should be further investigated for the delivery and toxicity of drug−HSA interactions.</p>\",\"PeriodicalId\":16531,\"journal\":{\"name\":\"Journal of Molecular Recognition\",\"volume\":\"36 8\",\"pages\":\"\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2023-05-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Recognition\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3040\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Recognition","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3040","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

采用等温滴定量热法(ITC)和硅对接计算研究了Cibacron Blue-F3GA (CB-F3GA)与人血清白蛋白(HSA)在生理低10倍浓度下的结合相互作用。ITC实验显示hb - f3ga在HSA上有两个不同的结合位点,它们对hb - f3ga具有不同的结合亲和力。HSA上的高亲和力结合位点(PBS-II)在纳米摩尔尺度(KD1 = 118±107 nM)与CB-F3GA结合,具有良好的结合焓(ΔHo1 =−6.47±0.44 kcal/mol)和熵(−TΔSo1 =−2.98 kcal/mol)能。CB-F3GA在μM尺度上(KD2 = 31.20±18.40 μM)结合在低亲和位点PBS-I上,具有良好的结合焓(ΔHo1 =−5.03±3.86 × 10−2 kcal/mol)和熵(−TΔSo1 =−1.12 kcal/mol)能。ITC结合数据强烈提示,CB-F3GA与PBS-II位点的结合增加了二聚体- hsa簇的形成(N1 = 2.43±0.50),而与PBS-I位点的结合导致四聚体- hsa簇的形成(N2 = 4.61±0.90)。这些结果表明,在生理条件下,HSA在药物结合时可能会有更高程度的聚集,这一概念应该进一步研究药物- HSA相互作用的传递和毒性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Isothermal titration calorimetry binding properties of Cibacron Blue F3GA in complex with human serum albumin

Binding interactions between Cibacron Blue-F3GA (CB-F3GA) and human serum albumin (HSA, at physiologically ten-fold lower concentration) was studied by isothermal titration calorimetry (ITC) and in-silico docking computations. ITC experiments revealed two separate binding sites on HSA with different binding affinities for CB-F3GA. The high-affinity binding site (PBS-II) on HSA binds CB-F3GA at nanomolar scale (KD1 = 118 ± 107 nM) with favorable binding enthalpy (ΔHo1 = − 6.47 ± 0.44 kcal/mol) and entropy (−TΔSo1 = −2.98 kcal/mol) energies. CB-F3GA binds to the low-affinity binding site (PBS-I) at μM scale (KD2 = 31.20 ± 18.40 μM) with favorable binding enthalpy (ΔHo1 = − 5.03 ± 3.86 × 10−2 kcal/mol) and entropy (−TΔSo1 = −1.12 kcal/mol) energies. ITC binding data strongly suggest that CB-F3GA binding to PBS-II site increases the formation of dimeric-HSA clusters (N1 = 2.43 ± 0.50), while binding to PBS-I leads to tetrameric-HSA clusters (N2 = 4.61 ± 0.90). These results suggest that a higher degree of HSA aggregation upon drug binding may be expected under physiological conditions, a notion that should be further investigated for the delivery and toxicity of drug−HSA interactions.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
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.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信