Fluorescence spectroscopy of osthole binding to human serum albumin
The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The...
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| Main Authors: | , , , , , |
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| Format: | Book |
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Elsevier,
2013-06-01T00:00:00Z.
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| Online Access: | Connect to this object online. |
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| Summary: | The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ÎH0, ÎG0 and ÎS0 were calculated at different temperatures. The results indicated that electrostatic forces played a major role in the interaction of osthole with HSA. Results of osthole synchronous fluorescence and UV absorption spectra showed that the microenvironment and conformation of HSA were changed. Keywords: Osthole, Human serum albumin, Fluorescence quenching |
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| Item Description: | 2095-1779 10.1016/j.jpha.2012.10.002 |