2013 Fiscal Year Final Research Report
Are inhalation anesthetics really receptor-binding drugs? : calorimetry of firefly luciferase
| Project/Area Number |
24659698
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Anesthesiology/Resuscitation studies
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| Research Institution | The University of Tokushima |
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Principal Investigator |
MATSUKI Hitoshi 徳島大学, ソシオテクノサイエンス研究部, 教授 (40229448)
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| Co-Investigator(Kenkyū-buntansha) |
TAMAI Nobutake 徳島大学, 大学院ソシオテクノサイエンス 研究部, 准教授 (00363135)
GOTO Masaki 徳島大学, 大学院ソシオテクノサイエンス 研究部, 助教 (30507455)
NISHIMOTO Makoto 和歌山工業高等専門学校, 物質工学科, 助教 (70609057)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | ルシフェラーゼ / 吸入麻酔薬 / 脂肪酸 / アデノシン３リン酸 / 示差走査熱量測定 / 等温滴定熱量測定 / 特異的および非特異的相互作用 / 誘導適合 |
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| Research Abstract |
Interaction modes of ligands with firefly luciferase (FFL) were investigated by calorimetry to clarify the high anesthetic sensitivity of FFL. Results of differential scanning calorimetry of FFL solutions revealed that the effect of an anesthetic chloroform on the structural stability of FFL is in direct opposition to that of the competitive inhibitor decanoic acid, and that the anesthetic sensitivity of FFL is markedly enhanced in the presence of the substrate (ATP) or decanoic acid as compared with that in the absence of the ligand. Results of isothermal titration calorimetry showed that the binding mode of an anesthetic halothane with FFL is quite different from that of decanoic acid thermodynamically. Comparing these thermal results with the structural data obtained by X-ray crystallography, we concluded that the possibility that there exist the anesthetic binding sites in FFL is very low.
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Research Products
(15 results)
