Unknown

Dataset Information

0

STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS.

ABSTRACT: 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).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.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.It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force.

SUBMITTER: Wang H 

PROVIDER: S-EPMC5412182 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS.

Wang Haidong H   Shi Hailang H   Pang Jie J   Song Xingfa X   Xu Caiyun C   Sun Zengxian Z  

African journal of traditional, complementary, and alternative medicines : AJTCAM 20160929 6

<h4>Background</h4>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).<h4>Materials and methods</h4>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 t  ...[more]

Similar Datasets

Unknown Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods.
| S-EPMC6152408 | biostudies-literature
Unknown Spectroscopic and molecular modeling studies of binding interaction between bovine serum albumin and roflumilast.
| S-EPMC6118266 | biostudies-literature
Unknown Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA).
| S-EPMC6332075 | biostudies-literature
Unknown Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods.
| S-EPMC3742238 | biostudies-literature
Unknown Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling.
| S-EPMC7919476 | biostudies-literature
Unknown Spectroscopic, thermodynamic and molecular docking studies of bovine serum albumin interaction with ascorbyl palmitate food additive.
| S-EPMC5801535 | biostudies-literature
Unknown Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches.
| S-EPMC6702422 | biostudies-literature
Unknown Mechanistic interaction studies of synthesized ZIF-8 nanoparticles with bovine serum albumin using spectroscopic and molecular docking approaches.
| S-EPMC9209420 | biostudies-literature
Unknown Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin.
| S-EPMC5762212 | biostudies-literature
Unknown Interaction of virstatin with human serum albumin: spectroscopic analysis and molecular modeling.
| S-EPMC3359307 | biostudies-literature