High-speed Atomic Force Microscopy for Capturing Dynamic Behavior of Protein Molecules at Work

In the quest for the mechanism of protein functions, various key techniques and instruments have been developed. This is an era when scrutinizing a certain protein from various angles is becoming possible through combined knowledge of its structure and function. However, it is necessary to link these different aspects of a protein along a time axis, but no technology is available for tracing a protein in action, at high spatial and temporal resolutions. Atomic force microscopy made it possible for the first time to view a nanometer-scale world in an aqueous environment. In 2001, we developed the first-generation highspeed atomic force microscope (AFM) that could capture moving protein molecules on video at 80 ms/frame. Since then, we have been carrying out various efforts to increase its scan rate as well as to substantially reduce tip–sample interaction force. The reduction in this force is a key to making the high-speed AFM practically useful in life sciences. Various new techniques and devices developed in the past four years have brought the AFM to its second-generation stage. It can now capture weakly interacting protein molecules successively without disturbing their physiological function. Here, we report our efforts made over the past four years, the present capacity of the high-speed AFM, and our preliminary work on the next generation of the instrument. [DOI: 10.1143/JJAP.45.1897]

[1]  R Y Tsien,et al.  Controlling cell chemistry with caged compounds. , 1993, Annual review of physiology.

[2]  Zbyszek Otwinowski,et al.  The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.

[3]  Paul K. Hansma,et al.  Tapping mode atomic force microscopy in liquids , 1994 .

[4]  S. Lindsay,et al.  A magnetically driven oscillating probe microscope for operation in liquids , 1996 .

[5]  Calvin F. Quate,et al.  Atomic force microscopy for high speed imaging using cantilevers with an integrated actuator and sensor , 1996 .

[6]  M. Viani,et al.  Small cantilevers for force spectroscopy of single molecules , 1999 .

[7]  Paul K. Hansma,et al.  Fast imaging and fast force spectroscopy of single biopolymers with a new atomic force microscope designed for small cantilevers , 1999 .

[8]  T. Ando,et al.  A high-speed atomic force microscope for studying biological macromolecules , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[9]  Andrew G. Glen,et al.  APPL , 2001 .

[10]  Horn-Sen Tzou,et al.  SENSORS AND ACTUATORS , 2001 .

[11]  Todd Sulchek,et al.  Characterization and optimization of scan speed for tapping-mode atomic force microscopy , 2002 .

[12]  Daisuke Maruyama,et al.  A High-Speed Atomic Force Microscope for Studying Biological Macromolecules in Action , 2002, Chemphyschem : a European journal of chemical physics and physical chemistry.

[13]  Masashi Kitazawa,et al.  Batch Fabrication of Sharpened Silicon Nitride Tips , 2003 .

[14]  F. Allgöwer,et al.  A new control strategy for high-speed atomic force microscopy , 2003 .

[15]  D. Manstein,et al.  Molecular engineering of a backwards-moving myosin motor , 2004, Nature.

[16]  Ericka Stricklin-Parker,et al.  Ann , 2005 .

[17]  Toshio Ando,et al.  Active damping of the scanner for high-speed atomic force microscopy , 2005 .

[18]  Toshio Ando,et al.  Feed-Forward Compensation for High-Speed Atomic Force Microscopy Imaging of Biomolecules , 2006 .

[19]  Toshio Ando,et al.  High-Speed Atomic Force Microscopy for Studying the Dynamic Behavior of Protein Molecules at Work , 2006 .