Molecular properties and effects of the binding of physiological and pharmacological ligands to human serum albumin.

Rizzuti B., Bartucci R., Guzzi R.

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The binding of small ligands to human serum albumin, the most abundant protein in blood plasma, was investigated by using theoretical methods such as molecular dynamics and docking simulations, in combination with experimental techniques that included fluorescence, differential scanning calorimetry, and Fourier transform infrared spectroscopy. The compounds studied encompass physiological (fatty acids), pharmacological (ibuprofen, warfarin) and nutraceutical molecules (resveratrol). The overall results revealed previously unknown details of the binding modes and interactions of these ligands within the protein, and clarified some key aspects of the binding features of albumin that include stereoselectivity, domain specificity and stabilization effects.

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