Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin
摘要
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.
引用本文（GB/T 7714）
TongKuanXU, XingHalSHEN, NaLI, 等. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin[J]. 中国化学快报：英文版, 2005.
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