A New Glance on Microscopic Images

September 17, 2009

Atomic force microscopy is well-known even in the public as a versatile tool for the production of images on the nanoscale level. Kelvin probe force microscopy is a special type of this imaging technique named after Lord Kelvin. When brought to the market in 1991, a scientific description of how to interprete the images was delivered. To this, physicist Christine Baumgart, a doctoral student of the nanospintronics group at the research center Forschungszentrum Dresden-Rossendorf (FZD), has now added new features.

Christine Baumgart now discovered what exactly is measured by Kelvin probe force microscopy. It is the electric potential which is needed to move electrons or holes from the inside to the surface of a semiconductor. Her new findings will simplify the microscopic technique itself, and will lead to unambiguous and reproducible results concerning the structure and electronic properties of samples. Also, Kelvin probe force microscopy, which has been used mainly in materials science and semiconductor physics so far, is likely to become more attractive for other areas like biotechnology.

But how exactly does a Kelvin probe force microscope work? The tip is deflected by the electrostatic force between cantilever and sample when moved over the sample. By applying bias to the sample, electrons and holes are moved to the surface of the semiconductor and the electrostatic force decreases. The cantilever moves back to its original position and the applied bias is stored as the signal measured. To be more precise, there is a quantitative relation between the measured Kelvin bias and the difference between the calculated Fermi energy and respective semiconductor band edge independent of the work function of the probing microscope tip. Thus, Christine Baumgart’s novel explanation of how the Kelvin probe force microscope works elucidates why the signal depends on the bias necessary for injecting majority charge carriers towards the interface between insulator and semiconductor.

Original publication:

Baumgart C., Helm M., Schmidt H., (2009): Quantitativ dopant profiling in semiconducters: A Kelvin probe force microscopy model. DOI: 10.1103/PhysRevB.80.085305.

https://www.fzd.de

Schematic drawing of a Kelvin probe force microscopy probe above a doped semiconductor with a thin oxide layer (grey blue atomic layer). Occupied surface states at the interface between the oxide layer and the semiconductor are animated in red and the same number of unscreened dopant atoms is animated in dark blue. Left: The resulting asymmetric electric dipole causes the deflection of the probe. Center: By applying a bias mobile majority charge carriers are injected into the semiconductor (animated in orange) and screen the unscreened ionized dopant atoms. Right:  As a result the electrostatic force onto the cantilever vanishes. The cantilever moves back to its normal position. The applied bias is measured and depends on the concentration of dopant atoms. Picture: Sander Münster, Kunstkosmos

Schematic drawing of a Kelvin probe force microscopy probe above a doped semiconductor with a thin oxide layer (grey blue atomic layer). Occupied surface states at the interface between the oxide layer and the semiconductor are animated in red and the same number of unscreened dopant atoms is animated in dark blue. Left: The resulting asymmetric electric dipole causes the deflection of the probe. Center: By applying a bias mobile majority charge carriers are injected into the semiconductor (animated in orange) and screen the unscreened ionized dopant atoms. Right: As a result the electrostatic force onto the cantilever vanishes. The cantilever moves back to its normal position. The applied bias is measured and depends on the concentration of dopant atoms. Picture: Sander Münster, Kunstkosmos


Imaging Surface Charges on Individual Biomolecules

September 2, 2009
Kelvin Probe Force Microscopy schematic

Kelvin Probe Force Microscopy schematic

Surface charges play a key role in determining the structure and function of proteins, DNA and larger biomolecular structures. For example, negatively charged DNA strands electrostatically interact with histone proteins, transcription factors, or polymerases thereby influencing the read-out of genetic information and the development of cancer. Similarly, the central process of protein folding and protein interaction, often governed by charges, is the major factor in protein-folding diseases such as Alzheimer’s or Parkinson’s Disease. However, thus far there have been no experimental methods to spatially resolve the electrostatic surface potential of individual biological molecules. In general, the investigation of individual molecules can shed light on their dynamic behaviour or on static heterogeneity which is masked in ensemble measurements.

A collaborative effort between researchers from the London Centre for Nanotechnology (Bart W Hoogenboom), King’s College London (Carl Leung, Patrick Mesquida) and UCL Chemistry (Stefan Howorka, Helen Kinns) has led to the first measurements of the electrostatic surface potential of individual DNA and avidin molecules with nanometre resolution using Kelvin Probe Force Microscopy (KPFM) in air.

Kelvin Probe Force Microscopy (KPFM) can measure surface charges by contactless recording of the electrostatic force between a conductive Atomic Force Microscope tip and a biomolecule on a support. To achieve this, the AFM tip is simultaneously excited at its mechanical resonance frequency and by an electrical (AC) voltage. This periodic electrical voltage on the tip leads to a force between the tip and the charges on the biomolecule, which is recorded by means of a lock-in amplifier and nullified by the Kelvin mode feedback by applying a separate DC voltage (not shown). The polarity and magnitude of this DC voltage corresponds to the local surface charge profile (in mV) which is recorded simultaneously with the topography of the biomolecule.

The investigation led at the London Centre for Nanotechnology also show, for the first time, the surface potential of buffer salts shielding DNA molecules on a surface, which would not be possible with conventional ensemble techniques. It is anticipated that the ability to visualize the electrostatic surface potentials of individual proteins and DNA at molecular resolution will be an important tool in fundamental biophysical research and in the fields of biosensing and bio-nanoelectronics.

Original Publication:

Leung C, Kinns H, Hoogenboom BW, Howorka S, Mesquida P. (2009): Imaging surface charges of individual biomolecules.  Nano Lett. 2009 Jul;9(7):2769-73.

 http://www.london-nano.com