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J. Biol. Chem., Vol. 275, Issue 39, 30439-30444, September 29, 2000

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Inhaled Anesthetic Binding Sites in Human Serum Albumin^*

Roderic G. Eckenhoff^§, Charles E. Petersen^¶, Chung-Eun Ha^¶, and Nadhipuram V. Bhagavan^¶

From the  Department of Anesthesia, University of Pennsylvania Medical Center, Philadelphia, Pennsylvania 19104-4283 and the ^¶ Department of Biochemistry and Biophysics, John A. Burns School of Medicine, University of Hawaii, Honolulu, Hawaii 96822

Previous evidence suggests multiple anesthetic binding sites on human serum albumin, but to date, we have only identified Trp-214 in an interdomain cleft as contributing to a binding site. We used a combination of site-directed mutagenesis, photoaffinity labeling, amide hydrogen exchange, and tryptophan fluorescence spectroscopy to evaluate the importance to binding of a large domain III cavity and compare it to binding character of the 214 interdomain cleft. The data show anesthetic binding in this domain III cavity of similar character to the interdomain cleft, but selectivity for different classes of anesthetics exists. Occupancy of these sites stabilizes the native conformation of human serum albumin. The features necessary for binding in the cleft appear to be fairly degenerate, but in addition to hydrophobicity, there is evidence for the importance of polarity. Finally, myristate isosterically competes with anesthetic binding in the domain III cavity and allosterically enhances anesthetic binding in the interdomain cleft.

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