Ordered nano-structure of a stamped self-organized protein layer on a HOPG surface using a HFB carrier

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 84; no. 2; pp. 395 - 399
• Main Authors: Iwanaga, Atsushi, Asakawa, Hitoshi, Fukuma, Takeshi, Nakamichi, Momoka, Shigematsu, Sakurako, Linder, Markus B., Haruyama, Tetsuya
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2011
• Subjects: Adsorption; atomic force microscopy; binding proteins; Carrier Proteins - chemistry; Carriers; colloids; Defects; Drop-stamp; Droplets; Hydrophobin; layering; maltose; Maltose-Binding Proteins - chemistry; methods; Microscopy, Atomic Force; Molecular interface; nanomaterials; Nanostructure; Nanostructures - chemistry; Proteins; Proteins - chemistry; Self-organized protein layer; Solid surfaces; Surface chemistry; Surface Properties; Drop-stamp; Self-organized protein layer; Hydrophobin; Molecular interface
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2011.01.032

[Display omitted] ► Functional protein molecule (maltose binding protein, MBP) can be self-organized at air/water interface when it is genetically tagged with hydrophobin (HFBII) as molecular self-organizing carrier. ► MBP–HFBII forms self-organized mono-layer on a surface of the solution droplet. The MBP–HFBII layer can be stamped onto a solid material surface in self-organized form. ► If the MBP–HFBII fusion molecules and HFBII molecules are mixed in solution, MBP distribution can be controlled accurately on both the solution droplet surface and it stamped solid substrate surface. A groundbreaking method for ordered molecular layer preparation on a solid surface employing the drop-stamp method has been developed by us taking advantage of the characteristics of the HFB molecule as a self-organizer/adsorption carrier. It is a smart method which can be used to prepare a self-organized protein layer on a solid surface without unspecific adsorption or defects. In our previous report, we clarified the self-organizing nature of HFB-tagged protein molecules on a surface of a solution droplet. In this report, a protein layer was prepared on a HOPG surface by using the drop-stamp method with a maltose binding protein (MBP)-tagged HFBII molecule. The structure of the stamped protein layer was investigated using frequency modulation atomic force microscopy (FM-AFM) in a liquid condition. The FM-AFM images show that the drop-stamp method can prepare an ordered protein layer on a solid surface smartly. The drop-stamp method using a HFB carrier is a practical method which can be used to prepare an ordered protein layer on a solid substrate surface without unspecific adsorption defects.