Neodymium is applied widely in agriculture to improve crop nutrition and incidentally in fertilizers, yet little is known of its effect on the biological function of human serum albumin (HSA). The interaction of Nd 3+ to HSA has been investigated mainly by fluorescence spectra, UV-vis absorption spectra and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of HSA by Nd 3+ was a static quenching process and the binding constant is 5.71 × 10 4 L mol -1 and the number of binding sites is 1 at 292 K. The thermodynamic parameters (DH 0 = -20.79 kJ mol -1 , DG 0 = -26.58 kJ mol -1 , and DS 0 = 19.85 J mol -1 K -1 ) indicate that electrostatic effect between the protein and Nd 3+ is the main binding force. The distance r = 2.91 nm between donor (HSA) and acceptor (Nd 3+ ) was obtained according to Förster's nonradiative energy transfer. In addition, UV-vis, CD and synchronous fluorescence results showed that the addition of Nd 3+ changed the conformation of HSA.