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Vol. 54, Issue 4, 610-615, October 1998
Departments of Anesthesia and Physiology, University of
Pennsylvania Health System, Philadelphia, Pennsylvania 19104-4283
To determine whether specific or nonspecific interactions between
inhaled anesthetics and proteins are more likely to underlie anesthetic
actions, analysis of hydrogen/tritium exchange was used to measure
effects on the stability of two model proteins that had been previously
shown to bind anesthetics specifically (bovine serum albumin) or only
nonspecifically (myoglobin). The data indicated that stabilization of
albumin correlated with the potencies of a wide range of anesthetic
compounds significantly better than did destabilization of myoglobin.
In addition, sensitivity to nonanesthetics, isoflurane
stereoselectivity, and temperature and pressure effects all influenced
the stabilization of bovine serum albumin, but not the
destabilization of myoglobin, in a manner strongly supporting the
premise that specific binding interactions with protein targets
underlie anesthetic action. These observations significantly increase
the likelihood that such interactions can be found and optimized.
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