High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes

Ando, Toshio; Uchihashi, Takayuki; Fukuma, Takeshi

doi:10.1016/j.progsurf.2008.09.001

Cited by 485 publications

(407 citation statements)

References 248 publications

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“…The striation pattern has been observed previously and found to be due to the resonant vibration of the piezo tube scanner (e.g. [20][21][22][23][24]). Therefore, the dominant factor that limits the response speed of the system at 0.1 s per frame was the resonance of the piezo tube [14].…”

Section: (B)supporting

confidence: 64%

Imaging stability in force-feedback high-speed atomic force microscopy

Kim

Boehm

2013

Ultramicroscopy

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We studied the stability of force-feedback high-speed atomic force microscopy (HSAFM) by imaging soft, hard, and biological sample surfaces at various applied forces. The HSAFM images showed sudden topographic variations of streaky fringes with a negative applied force when collected on a soft hydrocarbon film grown on a grating sample, whereas they showed stable topographic features with positive applied forces. The instability of HSAFM images with the negative applied force was explained by the transition between contact and noncontact regimes in the force-distance curve. When the grating surface was cleaned, and thus hydrophilic by removing the hydrocarbon film, enhanced imaging stability was observed at both positive and negative applied forces. The higher adhesive interaction between the tip and the surface explains the improved imaging stability. The effects of imaging rate on the imaging stability were tested on an even softer adhesive Escherichia coli biofilm deposited onto the grating structure. The biofilm and planktonic cell structures in HSAFM images were reproducible within the force deviation less than ~0.5 nN at the imaging rate up to 0.2 s per frame, suggesting that the force-feedback HSAFM was stable for various imaging speeds in imaging softer adhesive biological samples.

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Section: (B)supporting

confidence: 64%

Imaging stability in force-feedback high-speed atomic force microscopy

Kim

Boehm

2013

Ultramicroscopy

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“…As a result, the timescales of experiments and simulations are now within about an order of magnitude. This gap can be bridged with the use of small AFM cantilevers, as Ando et al 31 demonstrated a small cantilever AFM system that can detect torsional vibrations while the cantilever was driven at 1 MHz.…”

Section: Discussionmentioning

confidence: 99%

A nanomechanical interface to rapid single-molecule interactions

Dong

Şahin

2011

Nat Commun

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single-molecule techniques provide opportunities for molecularly precise imaging, manipulation, assembly and biophysical studies. owing to the kinetics of bond rupture processes, rapid single-molecule measurements can reveal novel bond rupture mechanisms, probe singlemolecule events with short lifetimes and enhance the interaction forces supplied by single molecules. Rapid measurements will also increase throughput necessary for technological use of single-molecule techniques. Here we report a nanomechanical sensor that allows single-molecule force spectroscopy on the previously unexplored microsecond timescale. We probed bond lifetimes around 5 µs and observed significant enhancements in molecular interaction forces. our loading-rate-dependent measurements provide experimental evidence for an additional energy barrier in the biotin-streptavidin complex. We also demonstrate quantitative mapping of rapid single-molecule interactions with high spatial resolution. This nanomechanical interface may allow studies of molecular processes with short lifetimes and development of novel biological imaging, single-molecule manipulation and assembly technologies.

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“…The laboratory-built high-speed AFM apparatus is an extensively improved version of the previously reported one 6 . See a comprehensive review 7 for the instrument development including recent technical advances. AFM images were acquired in the tapping mode.…”

Section: Methodsmentioning

confidence: 99%

“…Atomic force microscopy (AFM) is a versatile technique to image proteins in liquids at sub-molecular resolution, but its poor temporal resolution has meant an availability of only static or slow time-lapse images of proteins [1][2][3][4][5] . In the last decade, various efforts have been carried out to increase the scan speed of AFM [6][7][8][9] .…”

mentioning

confidence: 99%

“…However, dynamic visualization of physiologically relevant conformational changes in proteins has been difficult because tip-sample interaction tends to interfere with the physiological functions. To solve this problem, a new method has recently been developed which allows fast and precise control of the tip-sample distance with a minimum load to the sample 7 . This report presents the first ever exemplification of dynamic imaging of a functioning biological sample.…”

mentioning

confidence: 99%

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High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin

et al. 2010

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Remarkably, the bR-bR interaction in the transiently formed assembly elicits both positive and negative cooperative effects on the decay kinetics as the initial bR recovers. By the bipolar nature of the cooperativity, however, the turnover rate of the phtocycle is maintained constant on average, irrespective of the light intensity.Thus, the direct and high-resolution visualization of dynamically acting molecules is a powerful new approach to gaining insight into elaborate bimolecular processes. 2 The biological function of proteins is closely associated with their ability to undergo structural changes. In many cases, these structural changes are triggered by external stimuli including pH, temperature, ligand binding, mechanical stress, and light.Although their direct real-space and real-time visualization is a straightforward approach to understanding the dynamic molecular processes, the lack of suitable techniques has precluded it. Atomic force microscopy (AFM) is a versatile technique to image proteins in liquids at sub-molecular resolution, but its poor temporal resolution has meant an availability of only static or slow time-lapse images of proteins [1][2][3][4][5] . In the last decade, various efforts have been carried out to increase the scan speed of AFM 6-9 .As a result, single protein molecules exhibiting Brownian motion are captured on video at a highest temporal resolution of ~30 ms 10 . However, dynamic visualization of physiologically relevant conformational changes in proteins has been difficult because tip-sample interaction tends to interfere with the physiological functions. To solve this problem, a new method has recently been developed which allows fast and precise control of the tip-sample distance with a minimum load to the sample 7 . This report presents the first ever exemplification of dynamic imaging of a functioning biological sample.Bacteriorhodopsin (bR) is a well-known example of the association between stimulus-triggered structural dynamics and biological function 11,12 , and its direct visualization has long been a goal. bR contains seven transmembrane α-helices (named A-G) enclosing the chromophore retinal 13,14 . In the photocycle, a series of spectral intermediates, designated J, K, L, M, N, and O, occur in that order 12 . The light-induced conformational changes in bR have been investigated by various methods 15-25 , leading to a consensus that the proton channel at the cytoplasmic surface is opened by the tilting of helix F away from the protein center 21,23,24 . Sass et al. reported helix F displacement of ~0.1 nm in the late M state, based on X-ray diffraction of the three-dimensional crystal of wild type (WT) 21 . However, a larger structural change in bR was reported in 3 the electron crystallography study of the D96G, F171C, F219L triple mutant of bR: displacement of helix F by ~0.35 nm away from the center of the protein 23 . The electron crystallography study of the F219L mutant further reported that helices E and F tilt away from the center of the protein, which is ...

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High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes

Cited by 485 publications

References 248 publications

Imaging stability in force-feedback high-speed atomic force microscopy

Imaging stability in force-feedback high-speed atomic force microscopy

A nanomechanical interface to rapid single-molecule interactions

High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin

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