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Interaction of Acrylodan with Human Serum Albumin. A Fluorescence Spectroscopic Study
Author(s) -
Moreno Fermin,
Cortijo Manuel,
GonzálezJiménez José
Publication year - 1999
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1999.tb08272.x
Subject(s) - fluorescence , chemistry , human serum albumin , albumin , human albumin , serum albumin , biochemistry , environmental chemistry , physics , optics
The binding of the fluorescent probe acrylodan (AC) to human serum albumin (HSA) was studied by fluorescence spectroscopy. The binding isotherms could be fitted to two types of sites. Competition experiments using io‐doacetamide suggested that AC binds tightly on HSA by the cysteine‐34. Attempts were made to find the location of the second site using high concentrations of warfarin, phenylbutazone, diazepam, indomethacin, palmitic acid or bilirubin in order to displace the bound AC to the HSA. Bilirubin was the only ligand able to displace the bound AC. This result suggests that AC, which is a very hydrophobic molecule also capable of labeling lysine residues, should also bind the human albumin in the primary site of bilirubin, but with less affinity than to the cysteine‐34.