Molecular characterization of the interaction between human serum albumin and ibuprofen.

Guglielmelli A., Rizzuti B., Guzzi R.
  Giovedì 14/09   09:00 - 11:30   Aula A209   V - Biofisica e fisica medica
The interaction between human serum albumin (HSA) and ibuprofen (IBP) has been characterized by using differential scanning calorimetry, attenuated total reflection infrared spectroscopy and molecular dynamics simulation at different temperatures. The results show that increasing concentration of ibuprofen (up to tenfold IBP:HSA molar ratio) improve the protein resistance to thermal denaturation without altering its secondary structure. In fact, the melting temperature increased by about 12 ${}^{\circ} C$ with respect to the unliganded HSA, and such a stabilization has an entropic character. Experiments performed by using only the S- isomer of IBP further elucidated the stereoselectivity in the binding interaction with HSA.