Abstract: Heterocyclic aromatic amines (HAAs)，as a kind of carcinogenic substance，is mainly generated in the thermal process of foods． The study of its interaction with transport proteins is important for revealing its toxicity in human bodies． The interaction between two common heterocyclic aromatic amines as 2-amino-3-methylimidazole［4，5-f］-quinoline (IQ)，9H-pyrido ［3，4-b］indole (Norharman) and bovine serum albumin (BSA) was studied with multi-spectroscopic methods． It shows that both heterocyclic aromatic amines can be spontaneously combined with BSA to quench the endogenous fluorescence，and the binding site is about one for both heterocyclic aromatic amines． The quenching mechanism of IQ to BSA is a combination of dynamic and static quenching，in most cases dynamic quenching is dorminant． The molecular interaction between IQ and BSA is mainly driven by a hydrophobic force． The quenching mechanism between Norharman and BSA is the static quenching of ground state complex formation，and the binding is driven by hydrogen bonding and van der Waals force． Both IQ and Norhar-man can cause the changes of BSA conformation，and the degree of conformational change caused by IQ is higher than that of Norharman． In addition，according to the principle of minimum energy，the binding site of HAAs and BSA was simulated by molecular docking．

Key words: heterocyclic aromatic amines, bovine serum albumin, multi-spectroscopic method, molecular doc-king, interaction