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Article: An Isothermal Titration Calorimetry Study on the Binding of Four Volatile General Anesthetics to the Hydrophobic Core of a Four-[alpha]-Helix Bundle Protein
- Article from:
- Biophysical Journal
- Article date:
- November 1, 2003
- Author:
CopyrightCopyright Biophysical Society Nov 2003. Provided by ProQuest LLC. (Hide copyright information)
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ABSTRACT
A molecular understanding of volatile anesthetic mechanisms of action will require structural descriptions of anesthetic-protein complexes. Previous work has demonstrated that the halogenated alkane volatile anesthetics halothane and chloroform bind to the hydrophobic core of the four-[alpha]-helix bundle (A[alpha]^sub 2^-L38M)^sub 2^ (Johansson et al., 2000, 2003). This study shows that the halogenated ether anesthetics isoflurane, sevoflurane, and enflurane are also bound to the hydrophobic core of the four-[alpha]-helix bundle, using isothermal titration calorimetry. Isoflurane and sevoflurane both bound to the four-[alpha]-helix bundle with K^sub d^ values of 140 ± 10 µM, ...