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PubMed1996

Nanotribology and Nanofabrication of MoO3 Structures by Atomic Force Microscopy

Atomic force microscopy was used to characterize the sliding of molybdenum oxide (MoO3) nanocrystals on single-crystal molybdenum disulfide (MoS2) surfaces. Highly anisotropic friction was observed whereby MoO3 nanocrystals moved only along specific directions of the MoS2 surface lattice. The energy per unit area to move the MoO3 nanocrystals along their preferred sliding direction was an order of magnitude less than required to slide macroscopic MoS2-bearing contacts. This extreme friction anisotropy was exploited to fabricate multicomponent MoO3 nanostructures. These reversibly interlocking structures could serve as the basis for devices such as mechanical logic gates.

Journal Article↗
PubMed1999

Probing Nanometer Structures with Atomic Force Microscopy.

Atomic force microscopy (AFM) can generate high-resolution images of the surface of biological specimens and can also probe the interactions between and within single macromolecules. Thus isolated heterogeneous biological structures can be studied in submolecular detail with AFM.

Journal Article↗
PubMed2000

Anisotropy of Surface Roughness on Aluminium Sheet Studied by Atomic Force Microscopy.

Atomic force microscope images of aluminium sheet are used to calculate the mean roughness Ra and the root mean square roughness Rq for different directions (theta) across the samples. The angle determined values of Ra(theta) and Rq(theta) are significantly lower in the rolling direction than in any other direction. The results provide a clear demonstration of the vector nature of surface roughness. Local features in an angle determined Ra(theta) profile are also compared with the positions of peaks and valleys in the matching topographical cross-section of the surface running at right angles to theta. It is further found that the distribution of z heights for an imaged sample is usually not Gaussian in shape unless the z heights are measured about mean lines constructed across the surface parallel with the rolling direction. The results are relevant for controlling lubrication performance in the aluminium rolling process.

Journal Article↗
PubMed2005

Nanowire probes for high resolution combined scanning electrochemical microscopy - atomic force microscopy.

We describe a method for the production of nanoelectrodes at the apex of atomic force microscopy (AFM) probes. The nanoelectrodes are formed from single-walled carbon nanotube AFM tips which act as the template for the formation of nanowire tips through sputter coating with metal. Subsequent deposition of a conformal insulating coating, and cutting of the probe end, yields a disk-shaped nanoelectrode at the AFM tip apex whose diameter is defined by the amount of metal deposited. We demonstrate that these probes are capable of high-resolution combined electrochemical and topographical imaging. The flexibility of this approach will allow the fabrication of nanoelectrodes of controllable size and composition, enabling the study of electrochemical activity at the nanoscale.

Journal Article↗
PubMed1994

Comparison of medical-grade ultrahigh molecular weight polyethylene microstructure by atomic force microscopy and transmission electron microscopy.

Atomic force microscopy is used to image the topography of surfaces of bulk medical-grade ultrahigh molecular weight polyethylene (UHMWPE). Comparison with transmission electron microscopy images demonstrates that the AFM can resolve the plate-like stacks of crystalline lamellae characteristic of UHMWPE without aggressive surface treatment. Surface preparation for the AFM must be carried out by cryomicrotomy at extremely low temperatures to prevent smearing of surface features. Chemically-etched surfaces of UHMWPE require substantially less surface preparation for AFM imaging.

Freeze Fracturing↗
PubMed2001

Measurement of the length of the a helical section of a peptide directly using atomic force microscopy.

Using atomic force microscopy (AFM), the length of the alpha-helix structure of poly-L-lysine was investigated by stretching the peptide directly, one molecule at a time. In the absence of urea, many rupturing points that seemed to be due to the breaking of some hydrogen bonds were observed in force-extension curves, while these points were never observed in the presence of 8 M urea. In the presence of 0.4 or 1.6 M urea, both force-extension curve types were observed. Total peptide elongation for each condition was calculated from force-extension curves reflecting the alpha-helix rupturing process. The experimental value of total elongation divided by the theoretical value of total alpha-helix elongation yields the alpha-helix content. This value was compatible with circular dichroism (CD) measurement results. This suggests that peptide conformation and content of the alpha-helix on a single molecule scale can be investigated by direct mechanical measurement using atomic force microscopy.

Circular Dichroism↗
PubMed2000

High Molecular Orientation in Mono- and Trilayer Polydiacetylene Films Imaged by Atomic Force Microscopy.

Atomically flat monolayer and trilayer films of polydiacetylenes have been prepared on mica and silicon using a horizontal deposition technique from a pure water subphase. Langmuir films of 10,12-pentacosadiynoic acid (I) and N-(2-ethanol)-10,12-pentacosadiynamide (II) were compressed to 20 mN/m and subsequently polymerized by UV irradiation at the air-water interface. Blue and red forms of the films were prepared by varying exposure times and incident power. Polymerization to the blue-phase films produced slight contractions of 2 and 5% for the films of II and I, respectively. Longer UV exposures yielded red-phase films with dramatic film contraction of 15 and 32% for II and I, respectively. The horizontal deposition technique provided transfer ratios of unity with minimal film stress or structure modification. Atomic force microscopy images revealed nearly complete coverage of the substrate with atomically flat films. Crystalline domains of up to 100 micrometers of highly oriented polydiacetylene molecules were observed. The results reported herein provide insight into the roles of molecular packing and chain orientations in converting the monomeric film to the polymerized blue and red phases. Copyright 2000 Academic Press.

Journal Article↗
PubMed2001

Surface biology of DNA by atomic force microscopy.

The atomic force microscope operates on surfaces. Since surfaces occupy much of the space in living organisms, surface biology is a valid and valuable form of biology that has been difficult to investigate in the past owing to a lack of good technology. Atomic force microscopy (AFM) of DNA has been used to investigate DNA condensation for gene therapy, DNA mapping and sizing, and a few applications to cancer research and to nanotechnology. Some of the most exciting new applications for atomic force microscopy of DNA involve pulling on single DNA molecules to obtain measurements of single-molecule mechanics and thermodynamics.

DNA↗
PubMed1996

High resolution surface structure of E. coli GroES oligomer by atomic force microscopy.

Using atomic force microscopy (AFM) in aqueous solution, we show that the surface structure of the oligomeric GroES can be obtained up to 10 angstroms resolution. The seven subunits of the heptamer were well resolved without image averaging. The overall dimension of the GroES heptamer was 8.4 +/- 0.4 nm in diameter and 3.0 +/- 0.3 nm high. However, the AFM images further suggest that there is a central protrusion of 0.8 +/- 0.2 nm high and 4.5 +/- 0.4 nm in diameter on one side of GroES which displays a profound seven-fold symmetry. It was found that GroEL could not bind to the adsorbed GroES in the presence of AMP-PNP and Mg2+, suggesting that the side of GroES with the central protrusion faces away from the GroEL lumen, because only one side of GroES was observed under these conditions. Based on the results from both electron and atomic force microscopy, a surface model for the GroES is proposed.

Bacterial Proteins↗
PubMed2005

Characterization of freshwater natural aquatic colloids by atomic force microscopy (AFM).

Atomic force microscopy (AFM) has been used to image and quantify riverine colloids in a quantitative and relatively nonperturbing manner. Three main classes of material have been imaged including fibrils (about 10 nm in diameter and 100 nm or more in length), discrete, near-spherical, small colloids primarily below 30-50 nm in diameter, and a surface film, of at least several nanometers thickness, which coatsthe entire mica surface within 30 min of exposure to river water. Colloid structure was found to vary as a function of pH, particularly at high pH. Substantially different structures were observed at high pH values, with the loss of the near-spherical colloids possibly due to rearrangement and aggregation. In addition,film thicknesses of up to 100 nm were estimated on the silicon nitride AFM cantilever after 30 h of deposition in the same water (unperturbed and size fractionated). The observation of these surface films has important implications for understanding the mechanisms by which colloids might bind trace elements. In particular, development of surface coatings implies that binding of pollutants (at least initial surface binding) may be dominated by adsorbed surface layers.

Adsorption↗
PubMed2003

Characterization of dynamic cellular adhesion of osteoblasts using atomic force microscopy.

BACKGROUND: Atomic force microscopy (AFM) can be used to visualize the cell morphology in an aqueous environment and in real time. It also allows the investigation of mechanical properties such as cell compliance as a function of cell attachment. This study characterized and evaluated osteoblast adhesion by AFM. METHODS: Human bone marrow stromal cells were cultured on two types of surface to induce weak and strong cellular adhesions. RESULTS: Cells were considered as spreading if they had a flattened and lengthened shape and a cytoskeletal organization in the submembrane cytosolic region. Cell detachment demonstrated different adhesion states between adherent cells to be distinguished. The stability of the cytoskeletal fibers indicated that cells were adherent. The elastic modulus was estimated by two complementary approaches. The values deduced were between 3 x 10(2) and 2 x 10(5) Nm(-2) according to the state of cell adhesion and the approaches used to measure this elastic modulus. CONCLUSIONS: Although the results were qualitative, a relation may be deduced between the elasticity of living cells as demonstrated by cytoskeletal organization and the state of cell adhesion. The technique could be used to determine the adhesion state of an adherent osteoblast observed under AFM.

Bone Marrow Cells↗
PubMed1997

Cell viability and probe-cell membrane interactions of XR1 glial cells imaged by atomic force microscopy.

As atomic force microscopy (AFM) imaging of live specimens becomes more commonplace, at least two important questions arise: 1) do live specimens remain viable during and after AFM, and 2) is there transfer of membrane components from the cell to the AFM probe during probe-membrane interactions? We imaged live XR1 glial cells in culture by single- or dual-pass contact or tapping-mode AFM, examined cell viability at various postimaging times, and report that AFM-imaged live XR1 cells remained viable up to 48 h postimaging and that cell death rates did not increase. To determine if nonlethal, transient interactions between the AFM probe and cell membrane led to transfer of XR1 cell membrane phospholipid components on the probe, we treated the scanned probes with the lipid-binding fluorophore FM 1-43. Confocal microscopy revealed that phospholipid membrane components did accumulate on the probe, and to a generally greater extent during contact-mode imaging than during tapping-mode imaging. Moreover, membrane accumulations on the probe were greater when live XR1 cells were damaged or perturbed, yet membrane did not accumulate in fluorescently detectable quantities during repeated "force curves" during control experiments. Taken together, our data indicate that although AFM imaging of live cells in culture does not affect long-term cell viability, there are substantial probe-membrane interactions that lead to transfer of membrane components to the probe.

Animals↗
PubMed2004

Heterogeneous cell mechanical properties: an atomic force microscopy study.

Atomic force microscopy (AFM) is a non-invasive microscopy to explore living biological systems like cells in liquid environment. Thus AFM is an appropriate tool to investigate surface chemical modification and its influence on biological systems. In particular, control over biomaterial surface chemistry can result in a regulated cell response. This report investigates the influence of adhesive and non-adhesive surfaces on the cell morphology and the influence of the cytoskeleton structure on the local mechanical properties. In this study, the main work concerns a thorough investigation of the height images obtained with an AFM as therecorded images provide the evolution of the mechanical properties of the cell as function of its local structure. Information on the cell elasticity due to the cytoskeleton organization is deduced when comparing the AFM tip indentation depth versus the distance between the cytoskeleton bundles for the different samples.

Cell Adhesion↗
PubMed2002

Optical interference artifacts in contact atomic force microscopy images.

Atomic force microscopy images are usually affected by different kinds of artifacts due to either the microscope design and operation mode or external environmental factors. Optical interferences between the laser light reflected off the top of the cantilever and the light scattered by the surface in the same direction is one of the most frequent sources of height artifact in contact (and occasionally non-contact) images. They are present when imaging highly reflective surfaces, or even when imaging non-reflective materials deposited onto reflective ones. In this study interference patterns have been obtained with a highly polished stainless steel planchet. The influence of these artifacts in surface roughness measurements is discussed, and a semi-quantitative method based on the fast Fourier transform technique is proposed to remove the artifacts from the images. This method improves the results obtained by applying the usual flattening routines.

Artifacts↗
PubMed2004

Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study.

Atomic force microscopy was employed to study ex vivo amyloid material isolated from the transplanted hearts of two patients affected by systemic amyloidosis caused by the Leu174Ser apolipoprotein A-I variant. The purified material consists of fibrils and globular aggregates. For both patients the same morphological patterns are observed; in addition, fibril diameters obtained for the two patients turn out to be compatible, both in air (2.00+/-0.02 and 2.04+/-0.04 nm) and under liquid (10.7+/-0.4 and 11.3+/-0.5 nm). Fibrils display heterogeneous morphologies, occasionally showing a left-handed twist. Inspection of fibril ends, the study of fibril contour shape and the analysis of partially unfolded fibrils yield independent evidences suggesting that most twisted fibrils are composed of three protofilaments. The size of globular aggregates is the same for both patients (4.4+/-0.4 and 5.1+/-0.5 nm, measured under liquid) and is compatible with the protofilament expected diameter, suggesting that globules may represent protofilament precursors.

Amyloid↗
PubMed2001

Characterisation of adhesional properties of lactose carriers using atomic force microscopy.

The atomic force microscopy (AFM) colloid probe technique was investigated as a method for the characterisation of adhesional properties of pharmaceutical powder surfaces. Lactose carriers used in dry powder inhaler (DPI) formulations were chosen for investigation since adhesion between the carrier surface and drug particles has been proposed to affect the dispersion of drug particles. Individual adhesion forces were determined by measuring the detachment forces in air between the colloid probe and the lactose particle surface. The colloid probe consisted of a silica sphere (10 microm diameter) attached to a V-shaped silicon nitride cantilever (spring constant, k=0.42 N/m). Adhesion forces were calculated from individual force-distance curves using Hooke's Law. Individual forces measured at various adhesion sites were observed to be reproducible and stable over 10 min (coefficient of variation, CV below 5%). The adhesion force distribution determined from measurements at multiple sites (n>50) on each sample followed a log-normal relationship (regression coefficient, r(2) ranged between 0.95 and 0.99). This enabled characterisation in terms of the geometric mean adhesion force and a geometric standard deviation (GSD). Significant differences (P<0.001) in adhesion force were observed between samples, ranging from 37.47+/-1.95 to 117.48+/-2.20 nN. This study demonstrates the suitability of AFM as sensitive technique for the characterisation of adhesional properties of pharmaceutical particles.

Adhesiveness↗
PubMed1999

Determining the molecular-packing arrangements on protein crystal faces by atomic force microscopy.

Previous atomic force microscopy (AFM) studies and periodic bond-chain (PBC) analyses of tetragonal lysozyme crystals have suggested that the (110) face consists of chains of molecules related to one another by 43 axes parallel to the crystal face. In this study, high-resolution AFM images of the (110) face were obtained and analyzed in order to verify this prediction. A computer program was employed which constructs the theoretical AFM image corresponding to a specific crystallographic molecular-packing arrangement and AFM tip shape. The packing arrangement and tip shape were varied in order to obtain the maximum possible correlation between experimental and theoretical images. The prediction from PBC analysis of an arrangement involving 43 helices was confirmed in this manner, while the alternate arrangement, consisting of molecules related to one another by 21 axes, was not observed. However, the surface structure was found to differ significantly even from this crystallographic arrangement. The molecules were found to pack slightly closer about what will become the 43 axes within the interior of the crystal, suggesting the occurrence of surface reconstruction or rearrangement on the tetragonal lysozyme (110) face. This study represents a new approach for more precise determination of the molecular-packing arrangements on protein crystal faces employing AFM.

Crystallization↗
PubMed1997

Mapping cell wall polysaccharides of living microbial cells using atomic force microscopy.

Functionalized atomic force microscope tips were used to sense specific forces of interaction between ligand-receptor pairs and to map the positions of polysaccharides on a living microbial cell surface. Gold-coated tips were functionalized with concanavalin A using a cross-linker with a spacer arm of 15.6 A. It was possible to measure the binding force between concanavalin A and mannan polymers on the yeast (Saccharomyces cerevisiae) cell surface. This force ranged from 75 to 200 pN. The shape of the force curve indicated that the polymers were pulled away from the cell surface for a fairly long distance that sometimes reached several hundred nanometres. The distribution of mannan on the cell surface was mapped by carrying out the force measurement in the force volume mode of atomic force microscopy (AFM). During the measurement, the maximum cantilever deflection after contact between the tip and the sample was kept constant at 10 nm using trigger mode to keep the pressing force on the sample surface as gently as possible at a force of 180 pN. This regime was used to minimize the non-specific adhesion between the tip and the cell surface. Specific molecular recognition events took place on specific areas of the cell surface that could be interpreted as reflecting a non-uniform distribution of mannan on the cell surface.

Cell Membrane↗