4.2 Article

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

Journal

PROTEIN JOURNAL
Volume 23, Issue 5, Pages 351-355

Publisher

SPRINGER
DOI: 10.1023/B:JOPC.0000032655.26249.ba

Keywords

acrylodan; albumin; energy transfer; prodan; promen

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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.

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