Resonance energy transfer between tryptophan-214 in human serum albumin and acrylodan, prodan, and promen.
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.
Instituto de Estudios Biofuncionales and Departamento de Fisicoquímica Farmacéutica, Universidad Complutense de Madrid, 28040 Madrid, Spain. jglezjne@ieb.ucm.es
José
J
González-Jiménez
Manuel
M
Cortijo
D015081:2-Naphthylamine / Q000031:analogs & derivatives* / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes / Q000737:chemistry*; D006801:Humans; D009281:Naphthalenes / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry*
D005456:Fluorescent Dyes; D009281:Naphthalenes; D012709:Serum Albumin; C120980:promen; C038517:prodan; C038518:acrylodan; D014364:Tryptophan; D015081:2-Naphthylamine