Abstract:

The interaction between sudanⅡand Myoglobin(Mb) was investigated via fluorescence spectroscopy. The experimental resultes suggest that there is strong interaction between sudanⅡand Mb. The binding site number n is about 1 and the binding constant, K is 3.84×10⁷L/mol. The position, type and energy of the interaction between sudanⅡand Mb were investigated by means of  the flexible molecule docking technology. It was obtained from the theoretical calculation that the values of potential energy, electrostatic energy and van der waals energy of the interaction between SudanⅡand Mb are -9419.9, -7468.8 and -1951.0 kJ/mol, respectively. SudanⅡcan form the hydrogen bonds with His64 of Mb. In addition,  SudanⅡcan also interact with Phe33 、Phe43、Phe106 and Phe138 residues, which can produce fluorescence. Thus, the interaction can lead to the fluorescence quenching of Mb. This is in good agreement with the result of the fluorescence experiments.

Key words: SudanⅡ, Myoglobin, Interaction, Molecule modeling