The Difference of Serum Protein Transport between Echinosides and Verbascoside | [Journal of Chemical Society of Pakistan • 2020]

Author(s):

1. Ming Guo: School of Science, Zhejiang Agricultural & Forestry University, Lin'an, China

2. Xiaoxue Zhao: School of Science, Zhejiang Agricultural & Forestry University, Lin'an, China

3. Peter. E. Brodelius: Department of Chemistry and Biomedical Sciences, Linnaeus University, 391 82 Kalmar, Sweden

4. Ling Fang: School of Science, Zhejiang Agricultural & Forestry University, Lin’an 311300, China

5. Zhihong Sun: School of Forestry and Bio-technology, Zhejiang Agricultural and Forestry University, Lin’an, Zhejiang, China

6. Rui Wang: School of Science, Zhejiang Agricultural & Forestry University, Lin’an 311300, China

Abstract:

Summary: Verbascoside (VER) is the enzymatic hydrolysis product of echinacoside (ECH). The molecular structures of ECH and VER have different glucosyl groups so they bind to serum albumin in different ways, resulting in different pharmacological actions. In this report, we have examined the binding characteristics between human serum albumin (HSA) and ECH/VER by molecular modeling and spectroscopic approaches. Molecular modeling revealed that VER bound to HSA mainly through hydrogen bonds, van der Waals forces and hydrophobic forces. The spectroscopic results showed that the interactions between HSA and VER/ECH involved a static binding process, and the bonding strength of the VER-HSA complex was stronger than that of the ECH-HSA complex. The value of the binding distances (r) was low, which indicated the occurrence of energy transfer. The reaction conformational pattern of HSA-VER and HSA-ECH gave a “two-state model” based on fluorescent phase diagram analysis. According to the thermodynamic model, the main forces between interaction of VER and HSA were hydrogen bonds and van der Waals forces, whereas the interaction between ECH and HSA was hydrophobic force. The fluorescence polarization analysis demonstrated that the interaction between HSA and VER or ECH generated a non-covalent complex. Compared with ECH, VER was more likely to bind with HSA because of its smaller molecular size and low polarity. The results of the spectral analysis concurred with the molecular modeling data, which provides a helpful reference for the study of the molecular reaction mechanism of VER/ECH binding to HSA.

Page(s): 369-382

DOI: DOI not available

Published: Journal: Journal of Chemical Society of Pakistan, Volume: 42, Issue: 3, Year: 2020

Keywords:

serum , albumin , Verbascoside , Echinacosid , Spectrum , Experiment , Molecular modeling

References:

References are not available for this document.

Citations

Citations are not available for this document.

Citations

Downloads

Views