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Intrinsic interaction mode of an inhalation anesthetic with globular proteins: a comparative study on ligand recognition |
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| Authors: | Makoto Nishimoto Ukyo Komatsu Nobutake Tamai Michio Yamanaka Shoji Kaneshina Kenji Ogli Hitoshi Matsuki |
| Affiliation: | 1. Department of Life System, Institute of Technology and Science, The University of Tokushima, 2-1 Minamijosanjima-cho, Tokushima, 770-8506, Japan 5. Department of Material Science, Wakayama National College of Technology, 77 Nada, Noshima, Gobo, Wakayama, 644-0023, Japan 2. Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, 2-1 Minamijosanjima-cho, Tokushima, 770-8506, Japan 3. Department of Chemistry, Faculty of Sciences, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, 812-8581, Japan 4. Division of Anesthesia and Emergency Medicine, Kaisei General Hospital, 3-5-28 Muro-machi, Sakaide, Kagawa, 762-0007, Japan |
| Abstract: | 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? |
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