Resonance energy transfer between tryptophan-214 in human serum albumin and acrylodan, prodan, and promen

被引:15
作者
González-Jiménez, J
Cortijo, M
机构
[1] Univ Complutense Madrid, Inst Estudios Biofunct, Madrid, Spain
[2] Univ Complutense Madrid, Dept Fis Quim Farmaceut, E-28040 Madrid, Spain
关键词
acrylodan; albumin; energy transfer; prodan; promen;
D O I
10.1023/B:JOPC.0000032655.26249.ba
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It has been proposed that acrylodan (6-acryloyl-2-dimethylaminonaphthalene) and prodan (6-propionyl-2-dimethylaminonaphthalene) bind to site I of human serum albumin, whereas promen (6-propionyl-2-methoxynaphthalene) binds to site II of this carrier protein. Because human albumin contains only one single tryptophan, at position 214, it has been possible to measure the distances from this amino-acid residue to each of the three probes by nonradiative energy transfer. The distances calculated, 2.97 +/- 0.10 nm, 3.14 +/- 0.11 nm, and 2.62 +/- 0.17 nm, respectively, confirm the locations previously proposed for all three probes.
引用
收藏
页码:351 / 355
页数:5
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