Intrinsic interaction mode of an inhalation anesthetic with globular proteins: a comparative study on ligand recognition

Interaction mode of an inhalation anesthetic halothane with water-soluble globular proteins, myoglobin (Mgb) and lysozyme (Lys), was studied by differential scanning calorimetry (DSC) and viscometry, and the results were compared with those of bovine serum albumin (BSA). The anesthetic sensitivity was markedly different among the proteins: Mgb was destabilized, Lys was slightly destabilized, and BSA was conversely stabilized. Further, the interaction mode was quite different from those of specific binders for the proteins. The anesthetic sensitivity was highly correlated with the hydrophilicity on the protein surface (Mgb