Abstract
The primary objective of this study is to evaluate the interactions of ellagic acid (EA) and oleuropein (OLE) with human serum albumin (HSA). Plasma protein binding model prediction and molecular modeling suggest that EA binds to HSA stronger than OLE, and that both interact with the binding pocket of HSA subdomain IIA. Furthermore, fluorescence spectroscopy confirmed that EA has a stronger HSA binding affinity than OLE. Three-dimensional fluorescence spectroscopy and CD spectroscopy, analyzed using DichroWeb, showed that the binding of EA and OLE to HSA induce conformational changes.
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