Binding properties of drospirenone with human serum albumin and lysozyme in vitro

• Interactions of DP with HSA and LYZ were studied by fluorescence quenching.
• Displacement experiments were used to find the mainly binding site in HSA.
• DP was found mainly bound in the active site hinge region of LYZ by docking methods.
• DP had different effects on the local conformation of HSA and LYZ.

The interaction of drospirenone (DP) with human serum albumin (HSA)/lysozyme (LYZ) was investigated using different optical techniques and molecular models. Results from the emission and time resolved fluorescence studies revealed that HSA/LYZ emission quenching with DP was initiated by static quenching mechanism. The LYZ–DP system was more easily influenced by temperature than the HSA–DP system. Displacement experiments demonstrated that the DP binding site was mainly located in site 1 of HSA. Based on the docking methods, DP was mainly bound in the active site hinge region where Trp-62 and Trp-63 are located. Conformation study showed that DP had different effects on the local conformation of HSA and LYZ molecules.

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