Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods
Bibliographic Data
| ID | 20347010 |
|---|---|
| Authors | Haidong Wang (0000-0003-4868-2373, The First People’s Hospital of Lianyungang), Hailang Shi (Xinjiang Medical University), Jie Pang (0009-0002-1789-7689, The First People’s Hospital of Lianyungang), Xingfa Song (The First People’s Hospital of Lianyungang), Caiyun Xu (0000-0002-3787-5893, The First People’s Hospital of Lianyungang), Zengxian Sun (0000-0003-2418-7917, The First People’s Hospital of Lianyungang) |
| Year | 2016 |
| Volume | 13 |
| Issue | 6 |
| Pages | 121-129 |
| Publication date | 2016-09-29 |
| Open Access | Yes |
| Type | ARTICLE |
| Venue | African Journal of Traditional Complementary and Alternative Medicines (JOURNAL) |
| Journal identifiers | ISSN: 0189-6016 • E-ISSN: 2505-0044 |
| Publisher | African Traditional Herbal Medicine Supporters Initiative (ATHMSI) (PUBLISHER) |
| DOI | 10.21010/ajtcam.v13i6.17 |
| PMID | 28480368 |
| OpenAlex | W2527781788 |
| Language | EN |
| References cited | 1 |
Background: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). Materials and Methods: The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. Results: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. Conclusion: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force
Binding constant · Binding site · Bovine serum albumin · Chromatography · Circular dichroism · Crystallography · Fluorescence · Hydrogen bond · Hydrophobic effect · Intermolecular force · Molecule · Triptolide · van der Waals force · Chemistry · Metal complexes synthesis and properties · Natural Compounds in Disease Treatment · Protein Interaction Studies and Fluorescence Analysis · Biochemistry · Organic Chemistry
| Highly cited | No |
|---|