フォトクロミックカンチレバーによる蛋白質の疎水・親水・荷電領域の可視化

Material type: 文書・図像類

Author: 安藤, 敏夫ほか

Publisher: 金沢大学理学部

Publication date: 2001-03-20

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Note (General)：: Atomic force microscope (AFM) was first invented as an imaging tool for nanometer worlds. However, it can be used also as a high-sensitive force senso...

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https://kaken.nii.ac.jp/search/?qm=50184320

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Material Type: 文書・図像類
Title: フォトクロミックカンチレバーによる蛋白質の疎水・親水・荷電領域の可視化
Author/Editor: 安藤, 敏夫
Aodo, Toshio
Author Heading: 安藤, 敏夫
Aodo, Toshio
Publication, Distribution, etc.: 金沢大学理学部
Publication Date: 2001-03-20
Publication Date (W3CDTF): 2001-03-20
Alternative Title: Visualization of Hydrophobic-, Hydrophilic-, and Charged Areas of Protein by Photochromic Cantilevers
Periodical title: 平成11(1999)年度科学研究費補助金基盤研究(C) 研究成果報告書 = 1999 Fiscal Year Final Research Report
No. or year of volume/issue: 1998-1999
Volume: 1998-1999
Pages: 33p.-
Text Language Code: jpn
Subject Heading: 蛋白質
力マップ
原子間力顕微鏡
フォトクロミック色素
カンチレバー
疎水性
親水性
電荷
Target Audience: 一般
Note (General): Atomic force microscope (AFM) was first invented as an imaging tool for nanometer worlds. However, it can be used also as a high-sensitive force sensor, which allows us to obtain a 2D map of forces exerted between a cantilever probe and sample surface. Adhesive, repulsive, rupture, or non-contact forces between an AFM probe and sample can tell us physicochemical properties of the sample such as hydrophobicity, hydrophilicity and electric charges, depending on the surface property of the probe used. To specify the physicochemical property of sample clearly it is best to scan the sample with probes having different properties. Yet, it is quite difficult to scan the same area of sample after changing cantilevers. This has been a main reason why AFM has not been successfully used for mapping property of protein surface. To detour this problem we developed an alternative method. Instead of changing cantilevers, we change the surface property of a photochromic probe by irradiating near-UV li ght. We synthesized a photochromic dye, vinyl malachite green (VMG) whose structure can change from hydrophobic to charged form on irradiation. This dye was attached to the tip of cantilever probes covalently. We also invented a scanning method to map rupture forces within a time shorter than an ordinary force-curve method. Although it was shorter, it still took 30 min, resulting in suffering from disturbance by mechanical and electrical drifts of the AFM.After confirming the usefulness of the photochromic probe in identifying physicochemical property of sample, we invented an additional scanning method to obtain non-contact force map and topography simultaneously. This method shortened the scan time to 5 min (although it is not short enough yet). The positive charges on a basic protein, lysozyme, was successfully visualized by this method. Parallel to these studies, we have developed a high-speed AFM.It can ultimately solve the problem that the observation of force map requires much longer time than topography. The frame rate for topography observation reached 2.5 frames/sec, about 250-times faster than ordinary AFM apparatus. Although we have not tried to use this new AFM for force mapping, its speed promises a few seconds of force mapping, and therefore in the near future we may be able to obtain much better resolution of force map on protein surfaces.
個々の蛋白質分子の疎水・親水・荷電各領域を原子間力顕微鏡(AFM)で可視化するための走査方法や装置の開発を行った。試料表面の異なる物理化学的性質を明確に同定するためには、それぞれの性質に対応するカンチレバープローブを用意しなければならない。カンチレバーを交換せねばならず、同じ試料領域をカンチレバーを交換して再度走査することは不可能である。そこで、光照射により疎水・荷電変換をするフォトクロミック色素をカンチレバーに導入するアイデアを導入した。カンチレバーを交換する必要がなく、異なる性質をもつプローブで同じ試料領域を繰り返し走査できる。カンチレバー探針に共有結合できるフォトクロミック色素(ビニルマラカイトグリーン(VMG))を先ず合成した。探針に導入したVMGでも疎水・荷電変換できることを確認した。走査時間を短縮できる吸着力マップ計測法とこのVMGプローブを用いて、試料表面の性質を明確に同定することに成功した。しかしながら、この走査は時間がかかり(30分)、装置のドリフトの影響を強く受ける。そこで、もっと走査時間を短縮できる(5分)非接触力計測によるマッピング法を開発し、蛋白質の電荷マッピングができることを示した。根本的に走査時間の短縮を図るために、AFM装置そのものの高速化することも行った。その結果通常の凹凸像観察で、250倍の高速化に成功した。この装置でのマッピングはまだ行っていないが、上述の走査手法及びVMGプローブの開発、及びこの高速AFMの開発により、蛋白質表面の物理化学的性質を精度よく高速にマッピングする道を拓いた。
研究課題/領域番号:10640384, 研究期間(年度):1998–1999
出典：「フォトクロミックカンチレバーによる蛋白質の疎水・親水・荷電領域の可視化」研究成果報告書　課題番号10640384(KAKEN：科学研究費助成事業データベース（国立情報学研究所）)　　　本文データは著者版報告書より作成
DOI: 10.24517/00034839
Access Restrictions: 限定公開
Related Material: https://kaken.nii.ac.jp/search/?qm=50184320
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-10640384/
https://kaken.nii.ac.jp/report/KAKENHI-PROJECT-10640384/106403841999kenkyu_seika_hokoku_gaiyo/
Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）
https://irdb.nii.ac.jp
Original Data Provider (Database): 金沢大学 : 金沢大学学術情報リポジトリKURA