Colloid and Polymer Science

, Volume 289, Issue 17–18, pp 1785–1797 | Cite as

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

  • Makoto Nishimoto
  • Ukyo Komatsu
  • Nobutake Tamai
  • Michio Yamanaka
  • Shoji Kaneshina
  • Kenji Ogli
  • Hitoshi MatsukiEmail author
Original Contribution


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 < Lys < BSA) and the rigidity of the protein structure (BSA ≈ Mgb < Lys). We showed that the anesthetic sensitivity among globular proteins can be roughly classified into four categories, and proteins with small hydrophilicity and soft structure are suitable as model proteins of anesthesia. By contrast, the binding of the specific binders was characterized by the lower effective concentrations. The molar ratio of the binder to the protein at the effective concentration was well consistent with the binding number determined from the X-ray structural analysis. Moreover, the interaction mode of the binder was not necessarily in accord with the mode expected from the change in the protein structure. Considering the above facts, we can systematically interpret the effect of an anesthetic on globular proteins by four factors: (1) hydrophobicity of an anesthetic, (2) hydrophilicity of a protein surface, (3) rigidity of a protein structure, and (4) molar ratio of an anesthetic to a protein at the effective concentration.


Differential scanning calorimetry Globular protein Inhalation anesthetic Specific and nonspecific interactions Specific binder Viscosity 



The authors all thank the late Professor Issaku Ueda at University of Utah for his encouragement and suggestions for researches of the molecular mechanism of anesthesia.


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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Makoto Nishimoto
    • 1
    • 5
  • Ukyo Komatsu
    • 2
  • Nobutake Tamai
    • 1
  • Michio Yamanaka
    • 3
  • Shoji Kaneshina
    • 1
  • Kenji Ogli
    • 4
  • Hitoshi Matsuki
    • 1
    Email author
  1. 1.Department of Life System, Institute of Technology and ScienceThe University of TokushimaTokushimaJapan
  2. 2.Department of Biological Science and Technology, Faculty of EngineeringThe University of TokushimaTokushimaJapan
  3. 3.Department of Chemistry, Faculty of SciencesKyushu UniversityHigashi-kuJapan
  4. 4.Division of Anesthesia and Emergency MedicineKaisei General HospitalSakaideJapan
  5. 5.Department of Material ScienceWakayama National College of TechnologyGoboJapan

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