Study on separation of protein molecules based on their selective
Project/Area Number |
21360021
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Thin film/Surface and interfacial physical properties
|
Research Institution | Yokohama National University |
Principal Investigator |
OGINO Toshio 横浜国立大学, 工学研究院, 教授 (70361871)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2011: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2010: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2009: ¥9,360,000 (Direct Cost: ¥7,200,000、Indirect Cost: ¥2,160,000)
|
Keywords | 固体表面 / タンパク質分子 / 分子認識 / 走査プローブ / ナノ構造 / タンパク質 / バイオインターフェース / 吸着 / 走査プローブ顕微鏡 / グラフェン / 静電相互作用 |
Research Abstract |
Single-crystalline sapphire surfaces treated under particular conditions exhibit a phase separation into hydrophilic and hydrophobic domains. Using this surface, we have studied interactions between solid surfaces and biomolecules. To clarify the chemical properties of the domain surfaces, we used scanning probe microscopy equipped with colloidal probes and measured adhesion forces between the probe colloids and the solid surfaces. We observed distinct differences in the chemical states between the hydrophilic and the hydrophobic domains. Then, we investigated the adsorption mechanism of various protein molecules and found that the major force in the molecule adsorption is electrostatic one. But, some experimental results suggest that hydrophobic interaction is also involved in the adhesion of proteins after their adsorption.
|
Report
(4 results)
Research Products
(196 results)