Citation: Yan WANG, Yan CHENG, Hong Fang SUN. Interaction of Nicotine and Bovine Serum Albumin[J]. Chinese Chemical Letters, ;2000, 11(3): 247-250. shu

Interaction of Nicotine and Bovine Serum Albumin

Division of Applied Chemistry, Department of Technical Physics, Peking University Beijing 100871

Received Date: 16 October 1999

Fund Project: We thank the financial support of The National Natural Science Foundation of China and Research Fund for Doctoral Program of Higher Education.

The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption,fluorescence,and ¹H NMR methods. With the addition of nicotine,the absorption band of BSA at about 210 nm decreased gradually,moved to longer wavelengths,and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The ¹H NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA's high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.
- Nicotine,
- BSA,
- UV absorption,
- fluorescence,
- ¹H NMR
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