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Vol. 49, Issue 4, 343-368, December 1997

Molecular Interactions Between Inhaled Anesthetics and Proteins

Roderic G. Eckenhoffa and Jonas S. Johansson

Departments of Anesthesia (R.G.E., J.S.J.), Physiology (R.G.E.), and Biochemistry and Biophysics (J.S.J.), and the Johnson Research Foundation (J.S.J.), University of Pennsylvania Medical Center, Philadelphia, Pennsylvania

I. Introduction
    A. General
    B. History
II. Anesthetic Binding to Protein
    A. Equilibrium Kinetics
    B. Thermodynamics
    C. Binding Forces
        1. The hydrophobic effect.
        2. Electrostatic interactions.
    D. Location and Character of Anesthetic Protein Binding Sites
        1. Functional and equilibrium binding assays.
        2. Spectroscopic approaches.
        3. Direct photoaffinity labeling.
        4. Crystallographic approaches.
        5. Molecular genetics.
        6. Binding site character summary.
III. Structural and Dynamic Consequences of Anesthetic Binding
    A. Secondary Structure
    B. Tertiary Structure
    C. Quaternary Structure
IV. Summary
Acknowldgments
References

a   Address for correspondence: R.G. Eckenhoff, M.D., Department of Anesthesia, 3400 Spruce Street, 7 Dulles Building, University of Pennsylvania Medical Center, Philadelphia, PA 19104-4283.

0031-6997/97/4904-0343$03.00/0
PHARMACOLOGICAL REVIEWS
Copyright © 1997 by The American Society for Pharmacology and Experimental Therapeutics


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