AI Article Synopsis
- The study examined how 5-Bromo-4-thio-2'-deoxyuridine (4-SBrdU) interacts with human serum albumin (HSA) using various spectroscopic techniques.
- Findings revealed that the interaction primarily involved dynamic fluorescence quenching, with hydrophobic interactions being the key force driving this interaction.
- The results from fluorescence experiments aligned well with those discovered through molecular docking simulations, indicating consistent outcomes across different methods.
Article Abstract
The interaction between 5-Bromo-4-thio-2'-deoxyuridine (4-SBrdU) and human serum albumin (HSA) was investigated by the methods of UV-vis absorbance, fluorescence and circular dichroism (CD) spectroscopy and molecular docking under simulative physiological conditions. The results showed that the quenching mechanism of HAS by 4-SBrdU was dynamic fluorescence quenching, hydrophobic interaction was the main intermolecular force based on thermodynamic data, the fluorescence experimental results were in agreement with results obtained by the molecular docking study.
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| http://dx.doi.org/10.1016/j.saa.2014.10.081 | DOI Listing |
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