Citation: Tong Kuan XU, Xing Hai SHEN, Na LI, Hong Cheng GAO. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin[J]. Chinese Chemical Letters, ;2005, 16(7): 943-946. shu

Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin

1.
College of Chemistry Engineering and Materials, Dalian Institute of Light Industry, Dalian 116034;
2.
College of Chemistry and Molecular Engineering, Peking University, Beijing 100871

Received Date: 16 August 2004

Fund Project: The work was supported by the National Natural Science Foundation of China (Grant No. 90206020, 29901001).

The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Forster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher,and the distance between tryptophan and 3H-indole is nearer.
- Substituted 3H-indole quaternary ammonium molecule,
- bovine serum albumin,
- fluorescence resonance energy transfer
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