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PubMed2005

Towards screening of inhalation formulations: measuring interactions with atomic force microscopy.

This review charts the progress of atomic force microscopy (AFM) to investigate particle interactions relevant to the performance of inhalers. AFM provides a unique opportunity to examine and quantify single particle behaviour of powdered drugs and excipients in a variety of environmental conditions. An introduction to AFM and particle interactions is given. Comparative experiments that rank adhesion between materials, and quantitative experiments that lead to the measurement of properties such as the work of adhesion and surface energy, are reviewed. The AFM has been widely used to investigate the effects of relative humidity and surface roughness on particle adhesion; these experiments are also reviewed. In the final section, the potential of this approach to screen formulations is discussed.

Administration, Inhalation↗
PubMed1999

Controlled unzipping of a bacterial surface layer with atomic force microscopy.

We have combined high-resolution atomic force microscopy (AFM) imaging and force spectroscopy to gain insight into the interaction forces between the individual protomers of the hexagonally packed intermediate (HPI) layer of Deinococcus radiodurans. After imaging the HPI layer, the AFM stylus was attached to individual protomers by enforced stylus-sample contact to allow force spectroscopy experiments. Imaging of the HPI layer after recording force-extension curves allowed adhesion forces to be correlated with structural alterations. By using this approach, individual protomers of the HPI layer were found to be removed at pulling forces of approximately 300 pN. Furthermore, it was possible to sequentially unzip entire bacterial pores formed by six HPI protomers. The combination of high-resolution AFM imaging of individual proteins with the determination of their intramolecular forces is a method of studying the mechanical stability of supramolecular structures at the level of single molecules.

Gram-Positive Cocci↗
PubMed1998

Scanning tunneling and atomic force microscopy probes of self-assembled, physisorbed monolayers: peeking at the peaks.

The imaging and control of self-assembled, physisorbed monolayers have been the subject of numerous scanning tunneling microscopy and atomic force microscopy investigations. The successful interpretation of the structures observed in scanning probe images of molecules self-assembled at liquid-solid and gas-solid interfaces has benefited greatly from recent experimental and theoretical work. These studies are converging on a general tunneling mechanism that accounts for the images of weakly bound, insulating adsorbates. Experiments in which the dynamical behavior of these monolayers has been monitored as a function of time both statically and after the introduction of an external perturbation are described, and novel studies of the selective control of monolayer structure that make use of internal and external electric fields, photons, and solvent coadsorption are reviewed.

Journal Article↗
PubMed2002

Lipid domain formation and ligand-receptor distribution in lipid bilayer membranes investigated by atomic force microscopy.

A novel experimental technique, based on atomic force microscopy (AFM), is proposed to visualize the lateral organization of membrane systems in the nanometer range. The technique involves the use of a ligand-receptor pair, biotin-avidin, which introduces a height variation on a solid-supported lipid bilayer membrane. This leads to a height amplification of the lateral membrane organization that is large enough to be clearly imaged by scanning AFM. The power of the technique is demonstrated for a binary dipalmitoylphosphocholine-diarachidoylphosphocholine lipid mixture which is shown to exhibit a distinct lateral lipid domain formation. The new and simple ligand-receptor-based AFM approach opens up new ways to investigate lipid membrane microstructure in the nanometer range as well as the lateral distribution of ligand-lipid and receptor-protein complexes in supported membrane systems.

Avidin↗
PubMed2001

Monitoring DNA immobilization and hybridization on surfaces by atomic force microscopy force measurements.

DNA immobilization and hybridization was carried out on Au substrates that were modified with mercaptopropanoic acid and then treated with aluminum(III) solution. The positively charged AI(III) film can be used to immobilize both ds-DNA and ss-DNA. Atomic force microscopy (AFM) was used to monitor the process by force measurements between a negatively charged silica tip and the substrates while immersed in dilute electrolyte. Surface hybridization of ss-DNA produces an increase in the surface charge and surface potential of the substrates, which is reflected by the increasing repulsive force as determined from AFM force-separation curves. A single-base mismatch was detectable in surface hybridization. The AFM force measuring technique was also employed to investigate the interaction of Ru(phen)3(2+) with ss-DNA and ds-DNA. The force measurement results showed that there is a small interaction between Ru(phen)3(2+) and ss-DNA, which was ascribed to the electrostatic binding of Ru(phen)3(2+) to the ss-DNA surface. For ds-DNA, there is a strong interaction which is believed to be due to the association or intercalation of Ru(phen)3(2+) with ds-DNA.

Base Sequence↗
PubMed2000

Celery (Apium graveolens L.) parenchyma cell walls examined by atomic force microscopy: effect of dehydration on cellulose microfibrils.

Atomic force microscopy (AFM) was used to image celery (Apium graveolens L.) parenchyma cell walls in situ. Cellulose microfibrils could clearly be distinguished in topographic images of the cell wall. The microfibrils of the hydrated walls appeared smaller, more uniformly distributed, and less enmeshed than those of dried peels. In material that was kept hydrated at all times and imaged under water, the microfibril diameter was mainly in the range 6-25 nm. The cellulose microfibril diameters were highly dependent on the water content of the specimen. As the water content was decreased, by mixing ethanol with the bathing solution, the microfibril diameters increased. Upon complete dehydration of the specimen we observed a significant increase in microfibril diameter. The procedure used to dehydrate the parenchyma cells also influenced the size of cellulose microfibrils with freeze-dried material having larger diameters than air-dried material.

Apiaceae↗
PubMed1994

Electron spectroscopy and atomic force microscopy studies of DNA adsorption on mica.

Various methods for the deposition of deoxyribonucleic acid (DNA) molecules on mica are investigated to determine their reproducibility, and to quantify their ability to bind DNA. The use of these deposition methods for sample preparation for biological scanning tunneling microscopy (STM) and atomic force microscopy (AFM) studies is discussed. Auger electron spectroscopy (AES) and electron spectroscopy for chemical analysis (ESCA) were used to investigate the quantity of DNA adsorbed. AFM images of DNA deposited using the methods investigated are presented. The combination of AFM results with AES and ESCA results provides a basic understanding of the deposition techniques studied and illustrates that electron spectroscopy can be a useful addition to studies of this nature.

Adsorption↗
PubMedDate not supplied

[Structural features of proteins by intermittent-contact atomic force microscopy].

Optimal conditions of protein scanning by atomic force microscopy were developed. Proteins of different molecular masses (950-11.5 kDa) and different three-dimensional organization were used to investigate the structural features of proteins. The most distinct images of proteins were obtained using a tip with the free amplitude in the range of 5-15 nm and with the set-point amplitude in the regime of repulsion from the sample. The method allowed one to clearly recognize the structural details of large molecules such as immunoglobulins IgM and IgG1 and Ricinus agglutinin. The revealing of the structural properties of proteins with molecular masses of 60 kDa and less was limited by the sharpness of probe tips used in the present study. It was shown that, by a quantitative analysis of the geometric parameters of molecules, it is possible to distinguish IgG1, Ricinus agglutinin, and ricin.

Immunoglobulin G↗
PubMed2005

Atomic force microscopy of bacterial communities.

This chapter discusses atomic force microscopy (AFM) for the benefit of microbiologists who are interested in using this technique to examine the structures and dynamics of bacteria. AFM is a powerful technique for imaging biological samples at the nanometer to micrometer scale under nondestructive conditions. In order to be imaged with AFM, bacteria must be supported by a surface, which presents challenges because many laboratory strains of bacteria are planktonic. Still, in nature many bacteria live at surfaces and interfaces. This chapter discusses the benefits and difficulties of different methods that have been used to support bacteria on surfaces for AFM imaging and presents two methods in detail used to successfully grow and image bacteria at solid-liquid and solid-air interfaces. Using these methods it is possible to study bacterial morphology and interactions in a native state. These explorations by AFM have important applications to the study of different kinds of bacteria, interfacial bacterial communities, and biofilms.

Aluminum Silicates↗
PubMedDate not supplied

[The use of atomic-force microscopy for the analysis of microbiological objects].

Atomic force microscopy (AFM) was used for the analysis of rickettsiae and viruses. The specificity of interaction was evaluated on the basis of the adsorption of the analyzed antigen on the polymer-antibody film. The film was formed and transferred onto highly oriented pyrolytic graphite (HOPG) by the method of Langmuir-Schaefer with the use of amphiphilic polymers, alkylated polyethyleneimines. According to the data of AFM, polymer-antibody film was 10-30 nm thick and had ruptures, uneven surface. AFM images of Coxiella burnetii, rotavirus and Venezuelan equine encephalitis virus, immunoadsorbed on the antibody film, were obtained. C.burnetii, due to their size equal to (700-900) x (300-500) x Z = 200 nm, were clearly visible on the underlying surface and could be directly counted. Individual virus particles (60-80 nm) cold not be identified on such surface. To analyze such preparations, the program of image analysis was developed. The program classified the registered image with a certain standard. This program determined the presence of virus antigen on the underlying affinity surface with a high degree of precision.

Adsorption↗
PubMed2005

Strategies and results of atomic force microscopy in the study of cellular adhesion.

Atomic Force Microscopy (AFM) provides a range of strategies for investigating living cell adhesion to the extracellular matrix, other cells or biomaterials in their native environment. This review surveys the results obtained from major studies using AFM for mechanical force evaluation in the cell, morphological visualization of the cell and studies of the cell's response to chemical or mechanical stress. Recently, the use of AFM has been broadened to obtain experimental information about cell adhesion molecules. Quantitative measurements of binding forces between adhesion proteins and their ligands in the cell or on a surface are presented. These analyses provide data on individual molecules and their resulting collective behaviour at the cell level. They significantly contribute to the characterisation of cellular adhesion with physical principles relating to biochemistry.

Animals↗
PubMed1998

Simultaneous height and adhesion imaging of antibody-antigen interactions by atomic force microscopy.

Specific molecular recognition events, detected by atomic force microscopy (AFM), so far lack the detailed topographical information that is usually observed in AFM. We have modified our AFM such that, in combination with a recently developed method to measure antibody-antigen recognition on the single molecular level (Hinterdorfer, P., W. Baumgartner, H. J. Gruber, K. Schilcher, and H. Schindler, Proc. Natl. Acad. Sci. USA 93:3477-3481 (1996)), it allows imaging of a submonolayer of intercellular adhesion molecule-1 (ICAM-1) in adhesion mode. We demonstrate that for the first time the resolution of the topographical image in adhesion mode is only limited by tip convolution and thus comparable to tapping mode images. This is demonstrated by imaging of individual ICAM-1 antigens in both the tapping mode and the adhesion mode. The contrast in the adhesion image that was measured simultaneously with the topography is caused by recognition between individual antibody-antigen pairs. By comparing the high-resolution height image with the adhesion image, it is possible to show that specific molecular recognition is highly correlated with topography. The stability of the improved microscope enabled imaging with forces as low as 100 pN and ultrafast scan speed of 22 force curves per second. The analysis of force curves showed that reproducible unbinding events on subsequent scan lines could be measured.

Aluminum Silicates↗
PubMed2006

Measuring the elasticity of clathrin-coated vesicles via atomic force microscopy.

Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). CCVs are multicomponent protein and lipid complexes of approximately 100 nm diameter that are implicated in many essential cell-trafficking processes. Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 +/- 30 k(B)T, i.e., approximately 20 times that of either the outer clathrin cage or inner vesicle membrane. Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function.

Clathrin-Coated Vesicles↗
PubMed2006

The effects of fluoride on the nanostructure and surface pK of enamel crystals: an atomic force microscopy study of human and rat enamel.

Atomic force microscopy (AFM) studies have revealed 30-40 nm-wide regular positively charged bands across maturation-stage rat enamel crystals. Low pH resolved these into positively charged spherical domains of approximately 30 nm diameter. Crystal surface pK values from adhesion force titrations were approximately 6.5. The effect of fluoride on this pK value and on the nanostructure of fluorosed human enamel crystals has not been reported. The nanostructure and surface chemistry (pK) of normal and fluorotic human and of fluoride-treated rat maturing enamel crystals was examined. Enamel was sectioned and polished, prior to examination, using AFM in height and friction modes. High-resolution height images revealed 30 nm-diameter spherical domains within crystals, arranged as layers of hexagons or as a shallow spiral. Fluorotic enamel showed similar, but less well ordered, nanodomains. These could represent an arrangement of original initiation sites or binding sites for modulating matrix proteins. Surface pK was derived from adhesion-force measurements between functionalized tips (OH or COOH) and crystal surfaces between pH 2 and pH 10. pK values of approximately 6.5 for normal crystals were reduced to approximately 5.5 after fluoride treatment. Reduction in surface pK by fluoride might indicate lowered protonation with possible effects on matrix protein binding.

Amelogenesis↗
PubMed2003

Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations.

Titin I27 shows a high resistance to unfolding when subject to external force. To investigate the molecular basis of this mechanical stability, protein engineering Phi-value analysis has been combined with atomic force microscopy to investigate the structure of the barrier to forced unfolding. The results indicate that the transition state for forced unfolding is significantly structured, since highly destabilising mutations in the core do not affect the force required to unfold the protein. As has been shown before, mechanical strength lies in the region of the A' and G-strands but, contrary to previous suggestions, the results indicate clearly that side-chain interactions play a significant role in maintaining mechanical stability. Since Phi-values calculated from molecular dynamics simulations are the same as those determined experimentally, we can, with confidence, use the molecular dynamics simulations to analyse the structure of the transition state in detail, and are able to show loss of interactions between the A' and G-strands with associated A-B and E-F loops in the transition state. The key event is not a simple case of loss of hydrogen bonding interactions between the A' and G-strands alone. Comparison with Phi-values from traditional folding studies shows differences between the force and "no-force" transition states but, nevertheless, the region important for kinetic stability is the same in both cases. This explains the correspondence between hierarchy of kinetic stability (measured in stopped-flow denaturant studies) and mechanical strength in these titin domains.

Computer Simulation↗
PubMed2005

How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations.

We present high-resolution atomic force microscopy (AFM) imaging of the single-ring mutant of the chaperonin GroEL (SR-EL) from Escherichia coli in buffer solution. The native GroEL is generally unsuitable for AFM scanning as it is easily being bisected by forces exerted by the AFM tip. The single-ring mutant of GroEL with its simplified composition, but unaltered capability of binding substrates and the co-chaperone GroES, is a more suited system for AFM studies. We worked out a scheme to systematically investigate both the apical and the equatorial faces of SR-EL, as it binds in a preferred orientation to hydrophilic mica and hydrophobic highly ordered pyrolytic graphite. High-resolution topographical imaging and the interaction of the co-chaperone GroES were used to assign the orientations of SR-EL in comparison with the physically bisected GroEL. The usage of SR-EL facilitates single molecule studies on the folding cycle of the GroE system using AFM.

Adsorption↗
PubMed2003

Characterization of particle-interactions by atomic force microscopy: effect of contact area.

PURPOSE: The purpose of this work was to compare adhesion forces, contact area, and work of adhesion of salbutamol sulphate particles produced using micronization and a supercritical fluid technique (solution-enhanced dispersion by supercritical fluids--SEDS) using atomic force microscopy (AFM). METHODS: Adhesion forces of individual particles of micronized and SEDS salbutamol against a highly orientated pyrolytic graphite surface were acquired in a liquid environment consistent with that of a pressurized metered dose inhaler. The forces were then related to contact area and work of adhesion. RESULTS: The raw adhesion force data for the micronized and SEDS material were 14.1 nN (SD 2.5 nN) and 4.2 nN (SD 0.8 nN), respectively. After correction for contact area, the forces per unit area were 13 mN/microm2 (SD 2.3 mN/microm2) and 3 mN/microm2 (SD 0.6 mN/microm2). The average work of adhesion was calculated using the Johnson-Kendall-Roberts theory and was found to be 19 mJm(-2) (SD 3.4 mJm(-2)) for the micronized particle and 4 mJm(-2) (SD 0.8 mJm(-2)) for the SEDS particle. CONCLUSIONS: It is possible to produce a three-dimensional representation of the contact area involved in the interaction and make quantitative comparisons between different particles. There was a lower force per unit area and work of adhesion observed for the SEDS material, possibly because of its lower surface free energy.

Albuterol↗
PubMed2001

Probing molecular interactions and mechanical properties of microbial cell surfaces by atomic force microscopy.

Knowledge of the surface properties of microbial cells is a key to gain a detailed understanding of their functions in the natural environment and to efficiently exploit them in biotechnological processes. In this paper, we present force-distance curves recorded, by atomic force microscopy (AFM) in aqueous solutions, on various microbial samples: reconstituted S-layers, whole fungal spores and several bacterial strains. The approach and retraction curves exhibited important differences--depending on the type of microorganism, on the physiological state (dormancy versus germination) and on the environmental conditions (ionic strength)--which were shown to reflect differences in long-range surface forces, adhesion forces and mechanical properties. These data illustrate the great potential of AFM force measurements to elucidate the physical properties of microbial cells and to understand, at the molecular level, biointerfacial phenomena such as cell adhesion and cell aggregation.

Cell Adhesion↗