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PubMed1995

Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy.

Topographs of two-dimensional porin OmpF crystals reconstituted in the presence of lipids were recorded in solution by atomic force microscopy (AFM) to a lateral resolution of 10 angstroms and a vertical resolution of 1 angstrom. Protein-protein interactions were demonstrated on the basis of the AFM results and earlier crystallographic findings. To assess protein-lipid interactions, the bilayer was modeled with kinked lipids by fitting the head groups to contours determined with AFM. Finally, two conformations of the extracellular porin surface were detected at forces of 0.1 nanonewton, demonstrating the potential of AFM to monitor conformational changes with high resolution.

Crystallography, X-Ray↗
PubMedDate not supplied

Direct observation of poly(3-hydroxybutyrate) depolymerase adsorbed on polyester thin film by atomic force microscopy.

Poly[(R)-3-hydroxybutyrate] (PHB) depolymerases adsorbed on poly(L-lactide) (PLLA) thin film were directly observed by atomic force microscopy (AFM). A PLLA thin film of 100 nm thickness was prepared on a silicon wafer by spin-cast method. The PLLA thin film was treated at 220 degrees C and quenched to room temperature, resulting in the formation of a completely amorphous film with a smooth surface. Then, the PHB depolymerases from Pseudomonas stutzeri YM1006 and Ralstonia pickettii T1 were dispersed on the amorphous PLLA thin film. Direct AFM observation has revealed that the PHB depolymerases bind in an elliptic shape on the surface of the PLLA thin film and that a small ridge is created around each enzyme molecule. After removal of the enzymes with 40% ethanol aqueous solution, small hollows were found on the PLLA thin film. These results suggest that a PHB depolymerase interacts with polyester molecules during their adsorption to make a hollow on the substrate surface.

Adsorption↗
PubMed2003

Modeling of adhesion in tablet compression--I. Atomic force microscopy and molecular simulation.

Adhesion problems during tablet manufacturing have been observed to be dependent on many formulation and process factors including the run time on the tablet press. Consequently, problems due to sticking may only become apparent towards the end of the development process when a prolonged run on the tablet press is attempted for the first time. It would be beneficial to predict in a relative sense if a formulation or new chemical entity has the potential for adhesion problems early in the development process. It was hypothesized that favorable intermolecular interaction between the drug molecules and the punch face is the first step or criterion in the adhesion process. Therefore, the rank order of adhesion during tablet compression should follow the rank order of these energies of interaction. The adhesion phenomenon was investigated using molecular simulations and contact mode atomic force microscopy (AFM). Three model compounds were chosen from a family of "profen" compounds. Silicon nitride AFM tips were modified by coating a 20-nm iron layer on the surfaces by sputter coating. Profen flat surfaces were made by melting and recrystallization. The modified AFM probe and each profen surface were immersed in the corresponding profen saturated water during force measurements using AFM. The work of adhesion between iron and ibuprofen, ketoprofen, and flurbiprofen in vacuum were determined to be -184.1, -2469.3, -17.3 mJ. m(-2), respectively. The rank order of the work of adhesion between iron and profen compounds decreased in the order: ketoprofen > ibuprofen > flurbiprofen. The rank order of interaction between the drug molecules and the iron superlattice as predicted by molecular simulation using Cerius(2) is in agreement with the AFM measurements. It has been demonstrated that Atomic Force Microscopy is a powerful tool in studying the adhesion phenomena between organic drug compounds and metal surface. The study has provided insight into the adhesion problems occurring during tablet compression and a direction for continued study.

Adhesiveness↗
PubMed2006

Fungal surface remodelling visualized by atomic force microscopy.

Most fungal growth is localized to the tips of hyphae, however, early stages of spore germination and the growth of certain morphological mutant strains exhibit non-polarized expansion. We used atomic force microscopy (AFM) to document changes in Aspergillus nidulans wall surfaces during non-polarized growth: spore germination, and growth in a strain containing the hypA1 temperature sensitive morphogenesis defect. We compared wall surface structures of both wild-type and mutant A. nidulans following growth at 28 degrees and 42 degrees C, the latter being the restrictive temperature for hypA1. There was no appreciable difference in surface ultrastructure between wild-type and hypA1 spores, or hyphal walls grown at 28 degrees C. When dry mature A. nidulans conidia were wetted they lost their hydrophobin coat, indicating an intermediate stage between dormancy and swelling. The surface structure of hypA1 germlings grown at 42 degrees C was less organized than wild-type hyphae grown under the same conditions, and had a larger range of subunit sizes. AFM images of hyphal wall surface changes following a shift in growth temperature from restrictive (42 degrees C) to permissive (28 degrees C), showed a gradient of sizes for wall surface features similar to the trend observed for wild-type cells at branch points. Changes associated with the hyphal wall structure for A. nidulans hypA1 offer insight into the events associated with fungal germination, and wall remodelling.

Aspergillus nidulans↗
PubMed1999

Direct observation of oxidative stress on the cell wall of Saccharomyces cerevisiae strains with atomic force microscopy.

We imaged pores on the surface of the cell wall of three different industrial strains of Saccharomyces cerevisiae using atomic force microscopy. The pores could be enlarged using 10 mM diamide, an SH residue oxidant that attacks surface proteins. We found that two strains showed signs of oxidative damage via changes in density and diameter of the surface pores. We found that the German strain was resistant to diamide induced oxidative damage, even when the concentration of the oxidant was increased to 50 mM. The normal pore size found on the cell walls of American strains had diameters of about 200 nm. Under conditions of oxidative stress the diameters changed to 400 nm. This method may prove to be a useful rapid screening process (45-60 min) to determine which strains are oxidative resistant, as well as being able to screen for groups of yeast that are sensitive to oxidative stress. This rapid screening tool may have direct applications in molecular biology (transference of the genes to inside of living cells) and biotechnology (biotransformations reactions to produce chiral synthons in organic chemistry.

Antioxidants↗
PubMed2002

Atomic force microscopy study of the effects of Mg(2+) and other divalent cations on the end-to-end DNA interactions.

Atomic force microscopy (AFM) was applied to directly visualize the end-to-end DNA interaction mediated by magnesium cations. We took advantage of the APS-mica, allowing the preparation of samples in a broad range of monovalent and divalent cations to separate the effects of Mg(2+) and Na(+) cations on the interaction of restriction DNA fragments with cohesive end. The AFM data clearly show that DNA restriction fragments with cohesive ends form substantial amount of circles in the presence of Mg(2+) cations, suggesting that Mg(2+) cations stabilize the interaction of cohesive ends. This effect depends on the MgCl(2) concentration, so that the yield of circles approaches 18% in the presence of 50 mM MgCl(2). Furthermore, we demonstrate that this conferred cohesive end stability is specific for divalent cations, as substitution of MgCl(2) with NaCl leads to a near complete loss of cohesive end stability. We further demonstrate that cohesive end stabilization is achieved by substituting Mg(2+) with Ca(2+), Mn(2+), or Zn(2+). The data obtained suggest that the end stabilization mediated by divalent cations is primarily the result of inter-base interactions rather than bridging of phosphate moieties.

Cations, Divalent↗
PubMed2005

Atomic force microscopy investigation of chemically stabilized pericardium tissue.

Native and chemically stabilized porcine pericardium tissue was imaged by the contact mode atomic force microscopy (AFM), in air. Chemically stabilized pericardium is used as a tissue-derived biomaterial in various fields of the reconstructive and replacement surgery. Collagen type I is the main component of the fibrous layer of the pericardium tissue. In this study, the surface topography of collagen fibrils in their native state in tissue and after chemical stabilization with different cross-linking reagents: glutaraldehyde (GA), dimethyl suberimidate (DMS) and tannic acid (TA) was investigated. It has been found that chemical stabilization causes considerable changes in the surface topography of collagen fibrils as well as in the spatial organization of the fibrils within the tissue. The observed changes in the D-spacing pattern of the collagen fibril correspond to the formation of intrafibrilar cross-links, whereas formation of interfibrilar cross-links is mainly responsible for the observed tangled spatial arrangement of fibrils and crimp structure of the tissue surface. The crimp structure was distinctly seen for the GA cross-linked tissue. Surface heterogeneity of the cross-linking process was observed for the DMS-stabilized tissue. SDS-PAGE electrophoresis was performed in order to evaluate the stabilization effect of the tissues treated with the cross-linking reagents. It has been found that stabilization with DMS, GA or TA enhances significantly the tissue resistance to SDS/NaCl extraction. The relation between the tissue stability and changes in the topography of the tissue surface was interpreted in terms of different nature of cross-links formed by DMS, GA and TA with collagen.

Animals↗
PubMed2006

Photoswitching behavior of a novel single molecular tip for noncontact atomic force microscopy designed for chemical identification.

A tripod molecule with an azobenzene arm was designed as a single molecular tip for noncontact atomic force microscopy (NC-AFM). The azobenzene moiety showed photoisomerization that enabled measurements of the same position of the sample by different tip apexes with different interactions. Photoswitching behavior of the molecule synthesized and adsorbed on Au surfaces was examined and reversible switching between the trans- and cis forms was successfully confirmed by NC-AFM measurements.

Adsorption↗
PubMed2003

Atomic force microscopy and light scattering of small unilamellar actin-containing liposomes.

Three-dimensional networks of filamentous actin (F-actin) encapsulated inside phosphatidylcholine liposomes are currently being used in an effort to model the cytoskeleton and plasma membrane of eukaryotic cells. In this article, unilamellar lipid vesicles consisting of egg yolk-derived phosphatidylcholine encapsulating monomeric actin (G-actin) were made via extrusion in low ionic strength buffer (G-buffer). Vesicle shape and structure in these dispersions was studied using a combination of fluid-tapping atomic force microscopy, and multiangle static light scattering. After subjecting the liposome dispersion to high ionic strength polymerization buffer (F-buffer) containing K(+) ions, atomic force microscopy imaging and light scattering of these liposomes indicated the formation of specialized structures, including an overall liposome structure transformation from spherical to torus, disk-shaped geometries and tubular assemblies. Several atomic force microscopy control measurements were made to ascertain that the specialized structures formed were not due to free G-actin and F-actin self-assembling on the sample surface, plain liposomes exposed to G- and F-buffer, or liposomes encapsulating G-actin. Liposomes encapsulating G-actin assumed mostly thin disk shapes and some large irregularly shaped aggregates. In contrast, liposomes encapsulating polymerized actin assumed mostly torus or disk shapes along with some high aspect ratio tubular structures.

Actins↗
PubMed2000

Structural and topological differences between a glycopeptide-intermediate clinical strain and glycopeptide-susceptible strains of Staphylococcus aureus revealed by atomic force microscopy.

Novel cell surface topography was revealed on cocci from a glycopeptide-intermediate Staphylococcus aureus (GISA) clinical strain by using atomic force microscopy. The GISA isolate and its revertant had two parallel circumferential surface rings. One equatorial surface ring was observed in control strains. In vancomycin-susceptible strains, additional rings were formed in the presence of vancomycin. Ring depth measurements also revealed striking differences between the GISA strain and susceptible strains grown with or without vancomycin.

Anti-Bacterial Agents↗
PubMed2006

[Nanomanipulation of sections of human tongue squamous cell carcinoma by atomic force microscopy].

OBJECTIVE: To investigate the appropriate nanomanipulation of slides of human tongue squamous cell carcinoma tissue and cultured cells by atomic force microscopy (AFM), and develop methods to improve the resolution and contrast of AFM images. METHODS: Human tongue squamous carcinoma cells of the line Tca8113 were cultured. Cell masses were isolated and collected, and sectioned. Then the white lead and silvery white sections were transferred on mica slides, dried. Eighty slides were used and divided into 2 groups to be immersed into hydrogen dioxide of the concentrations 20% and 30% for 0, 5, 10, 15, 20, 25, 30, and 40 min respectively. Samples of human tongue squamous carcinoma were collected from 15 cases. Every sample was divided into 2 halves. Half of every sample underwent routine paraffin preparation of slide and adhered onto glass, dissolving of paraffin with dimethylbenzene for 0, 10, 15, 30, 45, or 60 min; and half of the sample underwent routine preparation of slides for electron microscopy, the white lead and silvery white sections were transferred on mica slides, dried. The slides were observed by contact mode AFM in air. RESULTS: In the ultrathin sections the metastructure of the cell such as the cell membrane, nuclear membrane and nucleolus could be distinct from each other clearly. The profile of the cell and the nucleus inside could be revealed by AFM after the paraffin sections were treated in dimethylbenzene for 15-30 min. AFM manipulation could be achieved within nanometer range by precise modulation of scanning force, area, angle and so on. The appropriate needle point should contain elastic coefficient > 5.0 N/m. The force exerted on the needle point should be within the range 50-300 nN. After location the scanning direction should be within the range of 20 nm-1 microm. CONCLUSION: A series of modified techniques of preparing and treating AFM samples, such as adhering the sections onto mica slide, dissolving of epoxy resin by hydrogen dioxide and removal of paraffin by dimethylbenzene, were developed, thus realizing high resolving power AFM imaging, especially for nuclear membrane, and nucleolus, and providing a base of AFM location, dissection, isolation and obtainment at nanometer scale.

Carcinoma, Squamous Cell↗
PubMed2000

Direct probing by atomic force microscopy of the cell surface softness of a fibrillated and nonfibrillated oral streptococcal strain.

In this paper, direct measurement by atomic force microscopy (AFM) of the cell surface softness of a fibrillated oral streptococcal strain Streptococcus salivarius HB and of a nonfibrillated strain S. salivarius HBC12 is presented, and the data interpretation is validated by comparison with results from independent techniques. Upon approach of the fibrillated strain in water, the AFM tip experienced a long-range repulsion force, starting at approximately 100 nm, attributed to the compression of the soft layer of fibrils present at the cell surface. In 0.1 M KCl, repulsion was only experienced when the tip was closer than approximately 10 nm, reflecting a stiffer cell surface due to collapse of the fibrillar mass. Force-distance curves indicated that the nonfibrillated strain, probed both in water and in 0.1 M KCl, was much stiffer than the fibrillated strain in water, and a repulsion force was experienced by the tip at close approach only (20 nm in water and 10 nm in 0.1 M KCl). Differences in cell surface softness were further supported by differences in cell surface morphology, the fibrillated strain imaged in water being the only specimen that showed characteristic topographical features attributable to fibrils. These results are in excellent agreement with previous indirect measurements of cell surface softness by dynamic light scattering and particulate microelectrophoresis and demonstrate the potential of AFM to directly probe the softness of microbial cell surfaces.

Biophysical Phenomena↗
PubMed2004

Mechanical properties and stability measurement of cholesterol-containing liposome on mica by atomic force microscopy.

The micromechanical properties of pure and cholesterol modified egg yolk phosphatidylcholine (EggPC) vesicles prepared by sonication were studied by atomic force microscopy (AFM) on mica surface. The force curves between an AFM tip and an unruptured vesicle were obtained by contact mode. During approach, two repulsion regions with two breaks were observed. The slopes of the two repulsive force regimes for the pure EggPC vesicles are determined to be several times lower than that of EggPC/cholesterol vesicles. The elastic properties from force plot analysis based on the Hertzian model showed that Young's modulus (E) and the bending modulus (kc) of cholesterol-modified vesicles increased several-fold compared with pure EggPC vesicles. The significant difference is attributed to the enhanced rigidity of the EggPC vesicles as a result of the incorporation of cholesterol molecules. The behavior of cholesterol-modified vesicles upon adsorption is different from that in solution as revealed by mechanical properties. The results indicate that AFM can provide a direct method to measure the mechanical properties of adsorbed small liposomes and to detect the stability change of liposomes.

Adsorption↗
PubMed2002

Experimental and numerical analyses of local mechanical properties measured by atomic force microscopy for sheared endothelial cells.

Local mechanical properties were measured for bovine endothelial cells exposed to shear stress using an atomic force microscopy (AFM), and the AFM indentations were simulated using a finite element method (FEM) to determine the elastic modulus. After exposure to shear stress, the endothelial cells showed marked elongation and orientation in the flow direction, together with significant decrease in the peak cell height. The applied force-indentation depth curve was obtained at seven different locations on the major axis of the cell surface and quantitatively expressed by the quadratic equation. The elastic modulus was determined by comparison of the experimental and numerical results. The modulus using our FEM model significantly became higher from 12.2+/-4.2 to 18.7+/-5.7 kPa with exposure to shear stress. Fluorescent images showed that stress fibers of F-actin bundles were mainly formed in the central portion of the sheared cells. The significant increase in the modulus may be due to this remodeling of cytoskeletal structure. The moduli using the Hertz model are 0.87+/-0.23 and 1.75+/-0.43 kPa for control and sheared endothelial cells respectively. This difference can be attributable to the differences in approximation functions to determine the elastic modulus. The elastic modulus would contribute a better understanding of local mechanical properties of the cells.

Animals↗
PubMedDate not supplied

MgATP-induced conformational changes in a single myosin molecule observed by atomic force microscopy: periodicity of substructures in myosin rods.

This paper discusses the conformational changes in a single myosin molecule directly observed using atomic force microscopy (AFM). The myosin molecules were pretreated in rigor solutions without MgATP or in relaxed solutions with various concentrations of MgATP. The images of these molecules were obtained using a tapping mode AFM. The results indicate that the orientation of the myosin's heads and tail strongly depend on the MgATP concentration. Without using MgATP, almost all of the myosin molecules are in the extended form; however, when MgATP is used, the molecules bend according to the level of MgATP concentration. The mean-square end-to-end distance of the myosin molecules is significantly shorter with p[MgATP] = 4 than with p[MgATP] = 6. The rod region did not show the same level of intensity along their length in the extended form. The rods exhibited clusters of discontinuity, which were identified as substructures. The size of these substructures change at intervals that are multiples of 14.3-14.5 nm, which reflects the periodicity of the alpha-helical coiled coils. The substructure clusters also correspond to the myosin crossbridge spacing in muscles (14.3 or 43 nm). These results suggest that the myosin's head bends in conjunction with the bending or tilting in the helical substructures. Conformational changes of the myosin molecule induced by MgATP seem to mimic the molecular motions in a muscle's force generation process.

Adenosine Triphosphate↗