Molecular interactions between inhaled anesthetics and proteins.
The fundamental interactions of inhalational anesthetics with proteins have been considered in some detail, using specific examples where appropriate to illustrate these interactions and demonstrate progress. It is now clear that these low-affinity volatile molecules with rapid kinetics can specifically bind to discrete sites in some proteins at reasonable pharmacological concentrations, and some general features of these sites are beginning to emerge. The structural or dynamic consequences of anesthetic binding, however, are still vague at best. The remaining challenge is to define which interactions produce anesthetic binding to relevant targets and what the features of this relevant anesthetic binding site are. Finally, and most importantly, how does the occupancy of these pockets, patches, or cavities result in the subtle alterations in protein conformation and dynamics that confound their function and ultimately produce the behavioral response that we term "anesthesia"?
Eckenhoff
R G
RG
Department of Anesthesia, University of Pennsylvania Medical Center, Philadelphia 19104-4283, USA.
Johansson
J S
JS
D018685:Anesthetics, Inhalation / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D007700:Kinetics; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D018685:Anesthetics, Inhalation; D011506:Proteins