How C60 Fullerenes Interact with Human Serum Albumin
Author Information
Author(s): Song Maoyong, Liu Shufang, Yin Junfa, Wang Hailin
Primary Institution: State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, China
Hypothesis
The study investigates how nC60 interacts with human serum albumin (HSA) and affects its structure and function.
Conclusion
The interaction between nC60 and HSA leads to fluorescence quenching and conformational changes in HSA, indicating functional changes in its drug binding sites.
Supporting Evidence
- The fluorescence intensity of HSA decreased with increasing concentration of nC60.
- The binding of HSA to nC60 increased the polar environment of the Trp residue, resulting in a red shift in the fluorescence spectra.
- The percentage of α-helicity of HSA increased upon association with nC60.
Takeaway
When tiny C60 particles mix with a protein called human serum albumin, they change how the protein looks and works, which might affect how it carries medicines in the body.
Methodology
The study used fluorescence, fluorescence dynamics, circular dichroism, and binding site marker competitive experiments to investigate the interaction.
Digital Object Identifier (DOI)
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