Fluorescence spectroscopy and UV-Vis absorption spectrometry assays were used to investigate the interaction mechanism of Fullerols and human serum albumin and bovine serum albumin under different temperature.The results revealed that Fullerols was capable of quenching SA’s fluorescence in both static modes. Binding constant values,binding site numbers and thermodynamics parameters of fixation reaction between Fullerols and serum albumin under different temperature were obtained with measurement and numeration. On the basis of thermodynamics data,the interaction forces of serum albumin after binding with Fullerols were mainly hydrophobic force.The binding strength of Fullerols and BSA was remarkably greater than that of Fullerols and HSA.Binding constants of Fullerols and BSA affected by temperature displayed dominant when bound to HSA. The binding sites of Fullerols and BSA were slightly larger.Then modes and mechanisms were observed by means of quenching mechanism analysis and molecular docking simulation method.Using AlignX amino acid Sequence Analys it was found that similarity of amino acid sequence of the two proteins were higher. Besides, significant difference in some small sequence fragments was observed.The distinctness was mostly in the vicinity of 160 and 185 of amino acid sequence,which proved that presumably affected the key sites of mode between the two proteins and Fullerols.