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

来源：

PROTEIN JOURNAL | 2004年 / 23卷 / 05期

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

页码：351 / 355

页数：5

共 34 条

[21] QUANTUM EFFICIENCIES OF FLUORESCENCE OF ORGANIC SUBSTANCES - EFFECT OF SOLVENT AND CONCENTRATION OF FLUORESCENT SOLUTE [J].