A. PÎRNĂU, M. BOGDAN

National R&D Institute for Isotopic and Molecular Technologies, 71–103 Donath str., 400293Cluj-Napoca, Romania

Human serum albumin (HSA), is the principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. This work was designed to examine the interaction of human serum albumin (HSA) with naproxen (NAP) in aqueous solution, using constant protein concentration of 1.25 μM and various naproxen contents of 4 –200 μM. UV-vis spectroscopy was used to determine the binding mode. The binding constant and the number of the binding sites were obtained using an identical independent-binding sites model, which assumes that each HSA molecule has n low-affinity binding sites, each with the same binding constant Kd.

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