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PubMed2002

Analysis of the formed track in solid state materials using atomic force microscopy.

The track formation in solid state materials, from the theoretical point of view, is still under study. One way to understand the track formation mechanisms and radiation damage of the charged particles in some materials such as polymers, glasses and minerals, is to analyse the surface topography effects. In this work, the track formation analysis in polycarbonate material is presented using an atomic force microscope (AFM) to characterise the evolution of the track on the material surface and beyond a thin layer of the surface material. The AFM is very useful to obtain valuable information at the level of the atomic structure of the materials and of the nuclear tracks, due to its high resolution and very easy operation involving also a simple sample preparation. The results show the development of the formed track by means of induced surface effects after being exposed to ionising radiation and chemical etching.

Microscopy, Atomic Force↗

PubMed2003

Humicola lanuginosa lipase hydrolysis of mono-oleoyl-rac-glycerol at the lipid-water interface observed by atomic force microscopy.

A new type of planar lipid substrate for Humicola lanuginosa lipase (HLL) has been prepared by depositing a monolayer of 1-mono-oleoyl-rac-glycerol (MOG) on top of a monolayer of dipalmitoyl-phosphatidylcholine (DPPC) on mica by the Langmuir-Blodgett (LB) technique. The bilayer was subsequently exposed to HLL in a liquid cell of an atomic force microscope (AFM) allowing the time course of the lipolytic degradation to be observed. By analysing a series of AFM images, we find that enzymes are preferentially activated at the edge of nano-scale defects present in the bilayer prior to enzyme injection, while defect-free areas of the substrate are surprisingly stable towards enzyme degradation. The initial rate of hydrolysis is found to be proportional to the perimeter length, P, of the initial nano-scale defects as well as the bulk enzyme concentration, c(HLL); d(lipid)/dt=k P c(HLL). We estimate the specific rate of MOG hydrolysis by HLL to be 2.5x10(4) MOG molecules/(minute x molecule of HLL).

1,2-Dipalmitoylphosphatidylcholine↗

PubMed2004

Imaging of the cortical cytoskeleton of guinea pig outer hair cells using atomic force microscopy.

Mammalian outer hair cells (OHCs) are known to respond to acoustical stimulation with elongation and contraction of the cells' cylindrical soma in vivo, and this motility is related to both the protein motors distributed along the OHC plasma membrane and the cytoskeleton beneath it. Therefore, the cytoskeleton seems to play an important role in the motility of the OHC. Recently, an atomic force microscope (AFM) was used to investigate the OHC cytoskeleton under physiological conditions. However, details were not made clear in that study. In this study, the ultrastructure of the cytoskeleton of fixed OHCs of guinea pigs, which were extracted with Triton X-100, was investigated using the AFM. As a result, the cortical cytoskeleton, which is formed by discrete oriented domains, was imaged, and circumferential filaments and cross-links were observed within the domain. Morphological change of the cytoskeleton of the OHC induced by diamide treatment was then examined using the AFM, and reduction of cross-links was observed. The examination indicates that the cortical cytoskeleton comprises circumferential actin filaments and spectrin cross-links.

Actin Cytoskeleton↗

PubMed1998

Differences in F9 and 5.51 cell elasticity determined by cell poking and atomic force microscopy.

We studied the elasticity of both a wild type (F9) mouse embryonic carcinoma and a vinculin-deficient (5.51) cell line, which was produced by chemical mutagenesis. Using cell poking, we measured the effects of loss of vinculin on the elastic properties of these cells. F9 cells were about 20% more resistant to indentation by the cell poker (a glass stylus) than were 5.51 cells. Using the atomic force microscope to map the elasticity of wild type and vinculin-deficient cells by 128 X 128 force scans, we observed a correlation of elasticity with cell poking elastometric measurements. These findings, as well as previous atomic force, rheologic, and magnetometric measurements [Goldmann and Ezzell, Exp. Cell Res. 226 (1996) 234-237; Ezzell et al., Exp. Cell Res. 231 (1997) 14-26], indicate that vinculin is an integral part of the cytoskeletal network.

Animals↗

PubMed1997

Surface dynamics in living acinar cells imaged by atomic force microscopy: identification of plasma membrane structures involved in exocytosis.

The dynamics at the plasma membrane resulting from secretory vesicle docking and fusion and compensatory endocytosis has been difficult to observe in living cells primarily due to limited resolution at the light microscopic level. Using the atomic force microscope, we have been able to image and record changes in plasma membrane structure at ultrahigh resolution after stimulation of secretion from isolated pancreatic acinar cells. "Pits" measuring 500-2000 nm and containing 3-20 depressions measuring 100-180 nm in diameter were observed only at the apical region of acinar cells. The time course of an increase and decrease in "depression" size correlated with an increase and decrease of amylase secretion from live acinar cells. Depression dynamics and amylase release were found to be regulated in part by actin. No structural changes were identified at the basolateral region of these cells. Our results suggest depressions to be the fusion pores identified earlier in mast cells by freeze-fracture electron microscopy and by electrophysiological measurements. The atomic force microscope has enabled us to observe plasma membrane dynamics of the exocytic process in living cells in real time.

Actins↗

PubMed2003

Ultrastructrural observation of the membrane surface of kainic acid-treated hippocampal neurons by atomic force microscopy.

OBJECTIVE: To observe the three-dimensional morphological changes on the membrane surface of primary cultured rat hippocampal neurons in response to kainic acid (KA) exposure. METHODS: After isolation and primary culture, Wistar rat hippocampal neurons were treated with KA at the concentrations of 0, 25, and 250 micromol/L for different durations (10 and 100 min) to observe the subsequent changes in the membrane surface structure of the neurons by nano-scale scanning with an atomic force microscope (AFM). RESULTS: Normal neurons displayed smooth membrane surface with even and regular undulation, while the neurons treated with KA, in contrast, presented degenerative changes characterized by cell swelling and coarse membrane surface with processes and holes. As the treatment was prolonged and KA concentration increased, the changes became more evident. CONCLUSION: As a result of the toxic effect of KA, the membrane surface ultrastructure of rat hippocampal neurons undergo obvious changes, which can be clearly observed and quantitatively analyzed by means of AFM.

Animals↗

PubMed2002

Structural heterogeneity of pyrimidine/purine-biased DNA sequence analyzed by atomic force microscopy.

We report here the direct evidence for the formation of alternative DNA structures in a plasmid DNA, termed pTIR10, containing a 0.23-kb pyrimidine/purine-biased (Pyr/Pur) stretch isolated from the rat genome. Long Pyr/Pur sequences are abundant in eukaryotic genomes, and they may modulate the biological activity of genes and genomes via formation of various types of triplex-related structures. The plasmid DNA in sodium acetate buffer (pH 4.35) was deposited on APS-modified mica, and after drying it was imaged with an atomic force microscope in air. Various types of thick protrusions have been observed on pTIR10 DNA. Structural parameters (width and height) of DNA molecules suggest that the alternative structures observed here are variations on the theme of an intramolecular triplex. The biological relevance of the structural features within Pyr/Pur stretches is discussed.

DNA↗

PubMed2005

Osteoblast elastic modulus measured by atomic force microscopy is substrate dependent.

The actin and microtubule cytoskeleton have been found to contribute to the elastic modulus of cells, which may be modulated by adhesion to extracellular matrix (ECM) proteins and subsequent alterations in the cytoskeleton. In this study, the apparent elastic modulus (Eapp) of osteoblast-like MC3T3-E1 cells adhered to fibronectin (FN), vitronectin (VN), type I collagen (COLI), fetal bovine serum (FBS), or poly-l-lysine (PLL), and bare glass were determined using an atomic force microscope (AFM). The E(app) of osteoblasts adhered to ECM proteins (FN, VN, COLI, and FBS) that bind cells via integrins were higher compared to cells on glass and PLL, which adhere cells through nonspecific binding. Also, osteoblasts adhered to FN, VN, COLI, and FBS had F-actin stress fiber formation, while osteoblasts on glass and PLL showed few F-actin fibers. Disruption of the actin cytoskeleton decreased E(app) of osteoblasts plated on FN to the level of osteoblasts plated on glass, while microtubule disruption had no significant effect. This suggests that the elevated modulus of osteoblasts adhered to FN was due to remodeling of the actin cytoskeleton upon adhesion to ECM proteins. Modulation of cell stiffness upon adhesion to various substrates may influence mechanosignal transduction in osteoblasts.

Actins↗

PubMed2003

Interactions between synaptic vesicle fusion proteins explored by atomic force microscopy.

Measuring the biophysical properties of macromolecular complexes at work is a major challenge of modern biology. The protein complex composed of vesicle-associated membrane protein 2, synaptosomal-associated protein of 25 kDa, and syntaxin 1 [soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) complex] is essential for docking and fusion of neurotransmitter-filled synaptic vesicles with the presynaptic membrane. To better understand the fusion mechanisms, we reconstituted the synaptic SNARE complex in the imaging chamber of an atomic force microscope and measured the interaction forces between its components. Each protein was tested against the two others, taken either individually or as binary complexes. This approach allowed us to determine specific interaction forces and dissociation kinetics of the SNAREs and led us to propose a sequence of interactions. A theoretical model based on our measurements suggests that a minimum of four complexes is probably necessary for fusion to occur. We also showed that the regulatory protein neuronal Sec1 injected into the atomic force microscope chamber prevented the complex formation. Finally, we measured the effect of tetanus toxin protease on the SNARE complex and its activity by on-line registration during tetanus toxin injection. These experiments provide a basis for the functional study of protein microdomains and also suggest opportunities for sensitive screening of drugs that can modulate protein-protein interactions.

Antigens, Surface↗

PubMedDate not supplied

Nanogel formation consisting of DNA and poly(amido amine) dendrimer studied by static light scattering and atomic force microscopy.

Binding of a poly(amido amine) dendrimer with salmon testes DNA in an aqueous solution of 0.01 M NaCl at pH 6.5 has been investigated. It was shown from the physicochemical experiments of static light scattering and ultra-violet and circular dichroism spectroscopy that at a 0.2 mixing ratio of dendrimer/DNA (number ratio of NH2 groups in dendrimer vs phosphate groups in DNA) significant conformational change of the DNA occurred owing to the binding of dendrimers on the DNA chain. The dendrimer/DNA complexes formed aggregates (nanogels) when the mixing ratio was increased above 0.2. Weight-averaged molecular weight, radius of gyration, and turbidity measurements revealed that the size of the aggregates increased up to a mixing ratio of 0.8. Atomic force microscopic images certified the formation of complexes and the morphology of the nanogels.

Animals↗

PubMed2006

Mapping the imprint of bone remodeling by atomic force microscopy.

Understanding bone remodeling is essential for understanding bone as a whole. Bone remodeling takes place through a stepwise cellular process, with osteoclasts carving small cavities, also known as resorption pits, into the surface of trabecular bone, followed by osteoblasts, which refill the pits with new soft bone collagen matrix tissue (osteoid). The detailed structure of the surface in the frontier of a resorption pit before, during, and after the osteoid is being laid down is not well known. We present detailed atomic force microscope (AFM) images from the edge, the front end, and the bottom of a resorption pit in a human trabecular bone sample that showed signs of incomplete remodeling. The images reveal a scalloped surface left behind by the osteoclasts and the surface morphology of preexisting bone tissue and new bone tissue. In addition, we display the bone formation front in the pit showing the anchor points between the new bone and the existing bone. We also found evidence of microcracking in the front end of the pit, suggesting that microcracking was the initiator of this particular resorption pit. We anticipate that AFM may initiate a more detailed understanding of the influence of the remodeling process on the structure of bone, as well as a better understanding of the surface on which new bone tissue can be anchored.

Aged↗

PubMed2004

Mechanical properties of sensory and supporting cells in the organ of Corti of the guinea pig cochlea--study by atomic force microscopy.

Mammalian hearing is refined by amplification of the motion of the cochlear partition. To understand the cochlear amplification, mechanical models of the cochlea have been used. When the dynamic behavior of the cochlea is analyzed by a model, elastic properties of the cells in the organ of Corti must be determined in advance. Recently, elastic properties of outer hair cells (OHCs) and pillar cells have been elucidated. However, those of other cells have not yet been clarified. Therefore, in this study, using an atomic force microscope (AFM), elastic properties of Hensen's cells, Deiters' cells and inner hair cells (IHCs) in the apical turn and those in the basal and second turns were estimated. As a result, slopes indicative of cell elastic properties were (8.9 +/- 5.8) x 10(3) m(-1) for Hensen's cells (n = 30), (5.5 +/- 5.3) x 10(3) m(-1) for Deiters' cells (n = 20) and (3.8 +/- 2.6) x 10(3) m(-1) for IHCs (n = 20), and Young's modulus were 0.69 +/- 0.45 kPa for Hensen's cells and 0.29 +/- 0.20 kPa for IHCs. There was no significant difference between elastic properties of each type of cell in the apical turn and those in the basal and second turns. However, it was found that there is a significant difference between Young's moduli of cells estimated in this study and those of the OHCs and pillar cells reported previously.

Animals↗

PubMed1994

Atomic force microscopy study of the collagen fibre structure.

Observations of intact reconstituted and native collagen fibres were performed with the atomic force microscope. The results are compared between the two types of fibres and with those obtained previously with the electron microscope on freeze-etched or negative stained samples. Some of the findings presented here indicate that the specimens observed in air with the atomic force microscope were still in a hydrated state.

Animals↗

PubMed1998

Effect of citric acid concentration on dentin demineralization, dehydration, and rehydration: atomic force microscopy study.

Most current dentin bonding procedures use acid etchants to partially demineralize the dentin structure and provide pathways for resin infiltration. This study determined the recession rates of peritubular dentin and intertubular dentin as a function of pH during demineralization in citric acid solutions (0.0005-2.5M) and the effects of dehydration and rehydration on the partially demineralized dentin. Polished dentin disks were prepared with an internal reference layer and were studied at specific intervals for citric acid etching between pH 1 and 3.4 in an atomic force microscope. Peritubular dentin etched rapidly and linearly with time until it could no longer be measured. The intertubular surface began etching at nearly the same rate, but then recession slowed for all concentrations and stabilized after recession of less than 1 microm for all but the pH 1 solution. The decrease in recession was attributed to the limitation of contraction of the demineralized collagen scaffold as long as it remained hydrated. Dehydration following etching resulted in significant collapse of the surface, changes in roughness, and a slight decrease in tubule diameter for samples etched for 30 min. Measurements could not be made of the collapse for low pH samples, because shrinkage stresses disrupted the integrity of the reference layer. On rehydration, the dehydrated surfaces underwent an expansion up to the level seen after etching and tubule diameters returned to the etched values. These results indicate that the collapse of demineralized matrix is almost totally recoverable on rehydration.

Citric Acid↗

PubMed1993

Identification of the elemental packing unit of DNA in mammalian sperm cells by atomic force microscopy.

DNA is packaged within the sperm cell nuclei of many vertebrates and all mammals in a highly condensed state by small basic proteins (protamines). Despite continuous investigation for nearly half a century, the actual packing arrangement of the DNA has remained unresolved. Atomic force and electron microscopy studies described in this report provide evidence that the fundamental packing unit for sperm DNA is a toroidal structure, 900A in outside diameter with a 150A diameter hole, which contains up to 60kb of DNA. Although the results presented here are based primarily upon investigations of mammalian sperm cells, they are expected to be valid for all sperm cells which utilize protamines to package DNA.

Animals↗

PubMed1991

Atomic force microscopy of a hydrated bacterial surface protein.

The protein surface layer of the bacterium Deinococcus radiodurans (HPI layer) was examined with an atomic force microscope (AFM). The measurements on the air-dried, but still hydrated layer were performed in the attractive imaging mode in which the forces between tip and sample are much smaller than in AFM in the repulsive mode or in scanning tunnelling microscopy (STM). The results are compared with STM and transmission electron microscopy (TEM) data.

Bacterial Proteins↗

PubMed2000

Adhesion forces measured by atomic force microscopy in humid air

Adhesive forces measured with an atomic force microscope under ambient conditions are generally regarded to be dominated by non-surface-specific capillary force. In this study, the nature of the "pull-off" force on a variety of surfaces was investigated as a function of relative humidity. The results indicate that even under the condition where capillary condensation occurs there is chemical specificity in the measured pull-off force. Issues such as tip-surface contact time and surface roughness were ruled out as possible artifacts. A mathematical model of pull-off force as a function of relative humidity is proposed in which the chemical specificity is explained.

Journal Article↗

PubMed2001

Demineralization of caries-affected transparent dentin by citric acid: an atomic force microscopy study.

OBJECTIVES: This study determined recession rates of peritubular dentin and intertubular dentin in citric acid solution (0.018M, pH=2.5) for caries-affected transparent dentin, one of the major components of dentin substrate as altered by caries, with comparisons made with non-carious dentin. METHODS: Transparent dentin was identified by sagittally sectioning five obviously carious teeth. Sections were then cut through the transparent dentin area perpendicular to the course of the dentinal tubules. Polished dentin samples of the transparent dentin and non-carious dentin were prepared with an internal reference layer and studied at specific intervals for citric acid etching in an atomic force microscope (AFM). RESULTS: At baseline, transparent dentin was identified by dentinal tubules that were largely occluded with mineral deposits that on etching proved to be acid resistant. Peritubular dentin etched rapidly and linearly over time until it could no longer be measured, yielding etching rates for transparent dentin that could not be distinguished from normal dentin. The normal and transparent intertubular dentin surfaces began etching at nearly the same rate, but then surface recession stabilized after less than 1 microm depth change for both dentin types. SIGNIFICANCE: Most previous studies have focused on demineralization and bonding to normal dentin, although many bonding procedures involve altered dentin substrates, such as those modified by caries. In this study, peritubular and intertubular dentin from normal and caries-affected dentin exhibited similar behavior. The major difference was the presence of acid resistant mineral in most of tubule lumens in the transparent dentin.

Acid Etching, Dental↗