Evaluating the interaction between di-fluorinated chalcones and plasmatic albumin
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文摘

The ligand-binding studies were performed by spectroscopy and molecular docking.

The samples follow combination of static and dynamic fluorescence quenching mechanism.

The Ka values indicate a moderate interaction between the ligands and albumin.

Hydrogen bonding and hydrophobic interactions are the main binding forces.

Changing the fluorine atoms position did not change the binding ability.

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