Abstract
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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González-Jiménez, J., Cortijo, M. Resonance Energy Transfer Between Tryptophan-214 in Human Serum Albumin and Acrylodan, Prodan, and Promen. J Protein Chem 23, 351–355 (2004). https://doi.org/10.1023/B:JOPC.0000032655.26249.ba
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DOI: https://doi.org/10.1023/B:JOPC.0000032655.26249.ba