Objective: To study the interaction of salbutamol sulfate (SAS) with human serum albumin (HSA) and human immunoglobulin G (HIgG). Method: Qualitative and quantitative structure changes of HSA and HIgG were performed by molecular modeling

UV-visible absorbance and circular dichroism spectroscopy methods. Result: The experiment results obtained from molecular modeling indicated that there were hydrogen bonds

Van der Waals force and electrostatic interactions between SAS and HSA;meanwhile

hydrogen bonds

π-cation interaction and Van der Waals force played the major role in the interaction of SAS and HIgG. Experimental results observed from UV-visible absorbance spectroscopy showed that the secondary structures of HSA and HIgG were altered in the presence of salbutamol sulfate

and their quenching mechanisms were both suggested as static quenching. Moreover

the α-helices of HSA in the presence of SAS were decreased from 47.92% to 46.53 %

and the secondary structure of HIgG was also changed because of the addition of salbutamol sulfate

which were obtained from the circular dichroism spectroscopy. Conclusion: Molecular modeling

UV-visible absorbance and circular dichroism spectroscopy are good methods for investigating the interaction between SAS

HSA and HIgG. They have the advantages of high speed and high sensitivity.