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 Matsuki

Research output: Contribution to journalArticle

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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 < 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.

Original languageEnglish
Pages (from-to)1785-1797
Number of pages13
JournalColloid and Polymer Science
Volume289
Issue number17-18
DOIs
Publication statusPublished - Nov 1 2011

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anesthetics
Inhalation Anesthetics
Anesthetics
respiration
Staphylococcal Protein A
Ligands
proteins
Proteins
ligands
Myoglobin
interactions
myoglobin
Muramidase
Bovine Serum Albumin
lysozyme
Binders
albumins
Hydrophilicity
serums
Enzymes

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Colloid and Surface Chemistry
  • Materials Chemistry

Cite this

Nishimoto, M., Komatsu, U., Tamai, N., Yamanaka, M., Kaneshina, S., Ogli, K., & Matsuki, H. (2011). Intrinsic interaction mode of an inhalation anesthetic with globular proteins: A comparative study on ligand recognition. Colloid and Polymer Science, 289(17-18), 1785-1797. https://doi.org/10.1007/s00396-011-2491-z

Intrinsic interaction mode of an inhalation anesthetic with globular proteins : A comparative study on ligand recognition. / Nishimoto, Makoto; Komatsu, Ukyo; Tamai, Nobutake; Yamanaka, Michio; Kaneshina, Shoji; Ogli, Kenji; Matsuki, Hitoshi.

In: Colloid and Polymer Science, Vol. 289, No. 17-18, 01.11.2011, p. 1785-1797.

Research output: Contribution to journalArticle

Nishimoto, M, Komatsu, U, Tamai, N, Yamanaka, M, Kaneshina, S, Ogli, K & Matsuki, H 2011, 'Intrinsic interaction mode of an inhalation anesthetic with globular proteins: A comparative study on ligand recognition', Colloid and Polymer Science, vol. 289, no. 17-18, pp. 1785-1797. https://doi.org/10.1007/s00396-011-2491-z
Nishimoto, Makoto ; Komatsu, Ukyo ; Tamai, Nobutake ; Yamanaka, Michio ; Kaneshina, Shoji ; Ogli, Kenji ; Matsuki, Hitoshi. / Intrinsic interaction mode of an inhalation anesthetic with globular proteins : A comparative study on ligand recognition. In: Colloid and Polymer Science. 2011 ; Vol. 289, No. 17-18. pp. 1785-1797.
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