Volatile anesthetics compete for common binding sites on bovine serum albumin: A 19F-NMR study

Brian W. Dubois, Sebastian F. Cherian, Alex S. Evers

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60 Scopus citations


There is controversy as to the molecular nature of volatile anesthetic target sites. One proposal is that volatile anesthetics bind directly to hydrophobic binding sites on certain sensitive target proteins. Consistent with this hypothesis, we have previously shown that a fluorinated volatile anesthetic, isoflurane, binds saturably [Kd (dissociation constant) = 1.4 ± 0.2 mM, Bmax = 4.2 ± 0.3 sites] to fatty acid-displaceable domains on serum albumin. In the current study, we used 19F-NMR T2 relaxation to examine whether other volatile anesthetics bind to the same sites on albumin and, if so, whether they vary in their affinity for these sites. We show that three other fluorinated volatile anesthetics bind with varying affinity to fatty acid-displaceable domains on serum albumin: halothane, Kd = 1.3 ± 0.2 mM; methoxyflurane, Kd = 2.6 ± 0.3 mM; and sevoflurane, Kd = 4.5 ± 0.6 mM. These three anesthetics inhibit isoflurane binding in a competitive manner: halothane, Ki (inhibition constant) = 1.3 ± 0.2 mM; methoxyflurane, Ki = 2.5 ± 0.4 mM; and sevoflurane, Ki = 5.4 ± 0.7 mM - similar to each anesthetic's respective Kd of binding to fatty acid displaceable sites. These results illustrate that a variety of volatile anesthetics can compete for binding to specific sites on a protein.

Original languageEnglish
Pages (from-to)6478-6482
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number14
StatePublished - Jul 15 1993


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