Study on the stereoselective binding of cytosine nucleoside enantiomers to human serum albumin
| Autor: | Cai Liu, Jingjing Guo, Fengling Cui |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Molecular model Stereochemistry Serum Albumin Human Cytidine 02 engineering and technology 010402 general chemistry 01 natural sciences Cytosine nucleoside Analytical Chemistry medicine Humans Instrumentation Spectroscopy Quenching (fluorescence) Chemistry Stereoisomerism 021001 nanoscience & nanotechnology Human serum albumin Atomic and Molecular Physics and Optics 0104 chemical sciences Molecular Docking Simulation Spectrometry Fluorescence Stereoselectivity Enantiomer 0210 nano-technology Hydrophobic and Hydrophilic Interactions Nucleoside Protein Binding medicine.drug |
| Zdroj: | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 224:117452 |
| ISSN: | 1386-1425 |
| DOI: | 10.1016/j.saa.2019.117452 |
| Popis: | Nucleoside drugs are known for their remarkable anticancer and antiviral properties. The development of nucleoside drugs has attracted much attention and generated a great deal of research interest. β-L-cytidine and β-D-cytidine are a pair of cytosine nucleoside enantiomers. In this work, the interactions between cytosine nucleoside enantiomers and human serum albumin were studied by ultraviolet-visible spectra, fluorescence spectrum and circular dichroism spectrum under simulated human physiological environment. The data of fluorescence spectra were corrected for the inner-filter effect to improve accuracy. Stern-Volmer quenching constants and binding constants in addition to thermodynamic parameters have been analyzed, which established that complexes formation have taken place via static quenching mechanism, and that hydrophobic force involved in these interactions. CD spectrum revealed that on addition of cytosine nucleoside enantiomers, the α-helix% of HSA increased slightly. What's more, molecular modeling method indicated that cytosine nucleoside enantiomers prefer binding at the IIIA site of HSA. |
| Databáze: | OpenAIRE |
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