کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1230607 | 1495240 | 2014 | 7 صفحه PDF | دانلود رایگان |

• Binding behavior of plant extract CVB to HSA was investigated.
• The thermodynamic parameters and structural information were obtained.
• Predicting the toxicity of CVB in the human plasma.
Cyclovirobuxine D is an active compound extracted from the plant Buxux microphylla, and widely available as medications; however, its abuse may casts potential detrimental effects on human health. By using multispectroscopic techniques and molecular modeling, the interaction of cyclovirobuxine D with human serum albumin was investigated. The fluorescence results manifested that static type was the operative mechanism for the interaction with human serum albumin. The structural investigation of the complexed HSA through CD, three-dimensional, FT-IR and synchronous fluorescence shown the polypeptide chain of HSA partially destabilizing. Docking studies revealed the molecule to be bound in the subdomain IIA. Finally, we investigated the distance between the bound ligand and Trp-214 of human serum albumin.
Molecular docking analysis of HSA with CVB.Figure optionsDownload as PowerPoint slide
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 128, 15 July 2014, Pages 552–558