PubMed Health⌕ Search

Biomedical subjects

Georg E Fantner

Publications and source records attributed to Georg E Fantner.

11 recordsLinked to original sources
PubMed2006

Hierarchical assembly of the siliceous skeletal lattice of the hexactinellid sponge Euplectella aspergillum.

Despite its inherent mechanical fragility, silica is widely used as a skeletal material in a great diversity of organisms ranging from diatoms and radiolaria to sponges and higher plants. In addition to their micro- and nanoscale structural regularity, many of these hard tissues form complex hierarchically ordered composites. One such example is found in the siliceous skeletal system of the Western Pacific hexactinellid sponge, Euplectella aspergillum. In this species, the skeleton comprises an elaborate cylindrical lattice-like structure with at least six hierarchical levels spanning the length scale from nanometers to centimeters. The basic building blocks are laminated skeletal elements (spicules) that consist of a central proteinaceous axial filament surrounded by alternating concentric domains of consolidated silica nanoparticles and organic interlayers. Two intersecting grids of non-planar cruciform spicules define a locally quadrate, globally cylindrical skeletal lattice that provides the framework onto which other skeletal constituents are deposited. The grids are supported by bundles of spicules that form vertical, horizontal and diagonally ordered struts. The overall cylindrical lattice is capped at its upper end by a terminal sieve plate and rooted into the sea floor at its base by a flexible cluster of barbed fibrillar anchor spicules. External diagonally oriented spiral ridges that extend perpendicular to the surface further strengthen the lattice. A secondarily deposited laminated silica matrix that cements the structure together additionally reinforces the resulting skeletal mass. The mechanical consequences of each of these various levels of structural complexity are discussed.

Animals↗
PubMed2006

Components for high speed atomic force microscopy.

Many applications in materials science, life science and process control would benefit from atomic force microscopes (AFM) with higher scan speeds. To achieve this, the performance of many of the AFM components has to be increased. In this work, we focus on the cantilever sensor, the scanning unit and the data acquisition. We manufactured 10 microm wide cantilevers which combine high resonance frequencies with low spring constants (160-360 kHz with spring constants of 1-5 pN/nm). For the scanning unit, we developed a new scanner principle, based on stack piezos, which allows the construction of a scanner with 15 microm scan range while retaining high resonance frequencies (>10 kHz). To drive the AFM at high scan speeds and record the height and error signal, we implemented a fast Data Acquisition (DAQ) system based on a commercial DAQ card and a LabView user interface capable of recording 30 frames per second at 150 x 150 pixels.

Animals↗
PubMed2005

Sacrificial bonds and hidden length: unraveling molecular mesostructures in tough materials.

Sacrificial bonds and hidden length in structural molecules and composites have been found to greatly increase the fracture toughness of biomaterials by providing a reversible, molecular-scale energy-dissipation mechanism. This mechanism relies on the energy, of order 100 eV, needed to reduce entropy and increase enthalpy as molecular segments are stretched after being released by the breaking of weak bonds, called sacrificial bonds. This energy is relatively large compared to the energy needed to break the polymer backbone, of order a few eV. In many biological cases, the breaking of sacrificial bonds has been found to be reversible, thereby additionally providing a "self-healing" property to the material. Due to the nanoscopic nature of this mechanism, single molecule force spectroscopy using an atomic force microscope has been a useful tool to investigate this mechanism. Especially when investigating natural molecular constructs, force versus distance curves quickly become very complicated. In this work we propose various types of sacrificial bonds, their combination, and how they appear in single molecule force spectroscopy measurements. We find that by close analysis of the force spectroscopy curves, additional information can be obtained about the molecules and their bonds to the native constructs.

Aggrecans↗
PubMed2005

Sacrificial bonds and hidden length dissipate energy as mineralized fibrils separate during bone fracture.

Properties of the organic matrix of bone as well as its function in the microstructure could be the key to the remarkable mechanical properties of bone. Previously, it was found that on the molecular level, calcium-mediated sacrificial bonds increased stiffness and enhanced energy dissipation in bone constituent molecules. Here we present evidence for how this sacrificial bond and hidden length mechanism contributes to the mechanical properties of the bone composite, by investigating the nanoscale arrangement of the bone constituents and their interactions. We find evidence that bone consists of mineralized collagen fibrils and a non-fibrillar organic matrix, which acts as a 'glue' that holds the mineralized fibrils together. We believe that this glue may resist the separation of mineralized collagen fibrils. As in the case of the sacrificial bonds in single molecules, the effectiveness of this mechanism increases with the presence of Ca2+ ions.

Animals↗
PubMed2004

High-resolution AFM imaging of intact and fractured trabecular bone.

Nanoscale structural analyses of biomineralized materials can frequently help elucidate important structure-function relationships in these complex organic-inorganic composites. Atomic force microscope (AFM) imaging of the exterior surface of trabecular bone reveals a densely woven structure of collagen fibrils, banded with a 67-nm periodicity, and densely packed mineral plates. The mineral plates on the collagen fibrils overlap and exhibit a large range of plate diameters from 30 to 200 nm. On the collagen fibrils, small nodular features, spaced 20-30 nm, run perpendicular to the fibrils. In some cases, these nodules are also seen on filaments extending between collagen fibrils. We hypothesize that these protrusions are noncollagenous proteins such as proteoglycans and may have collapsed into compact structures when the sample was dried. AFM images of pristine fractured surfaces reveal a dense array of mineral plates. In a few isolated locations, short sections of bare collagen fibrils are visible. In other regions, the existence of the underlying collagen fibrils can be inferred from the linear patterns of the mineral plates. Fractured samples, rinsed to remove mineral plates, reveal separated collagen fibrils on the fractured surfaces. These fibrils are often covered with protrusions similar to those observed on the exterior surfaces but are less organized. In addition, as on the exterior surfaces, there are sometimes small filaments extending between neighboring collagen fibrils. These studies provide important insights into the nanostructured architecture of this complex biocomposite.

Animals↗
PubMed2004

Influence of the degradation of the organic matrix on the microscopic fracture behavior of trabecular bone.

In recent years, the important role of the organic matrix for the mechanical properties of bone has become increasingly apparent. It is therefore of great interest to understand the interactions between the organic and inorganic constituents of bone and learn the mechanisms by which the organic matrix contributes to the remarkable properties of this complex biomaterial. In this paper, we present a multifaceted view of the changes of bone's properties due to heat-induced degradation of the organic matrix. We compare the microscopic fracture behavior (scanning electron microscopy; SEM), the topography of the surfaces (atomic force microscopy; AFM), the condition of bone constituents [X-ray diffraction (XRD), thermogravimetric analysis (TGA), and gel electrophoresis], and the macromechanical properties of healthy bovine trabecular bone with trabecular bone that has a heat-degraded organic matrix. We show that heat treatment changes the microfracture behavior of trabecular bone. The primary failure mode of untreated trabecular bone is fibril-guided delamination, with mineralized collagen filaments bridging the gap of the microcrack. In contrast, bone that has been baked at 200 degrees C fractures nondirectionally like a brittle material, with no fibers spanning the microcracks. Finally, bone that has been boiled for 2 h in PBS solution fractures by delamination with many small filaments spanning the microcracks, so that the edges of the microcracks become difficult to distinguish. Of the methods we used, baking most effectively weakens the mechanical strength of bone, creating the most brittle material. Boiled bone is stronger than baked bone, but weaker than untreated bone. Boiled bone is more elastic than untreated bone, which is in turn more elastic than baked bone. These studies clearly emphasize the importance of the organic matrix in affecting the fracture mechanics of bone.

Animals↗
PubMed2004

Rigid design of fast scanning probe microscopes using finite element analysis.

To improve the performance of atomic force microscopes regarding speed and noise sensitivity, it is important to consider the mechanical rigidity of the actuator (scanner), and the overall mechanical structure. Using finite element analysis in the design process, it was possible to increase the first resonance frequency from 950 Hz for the whole system to 23.4 kHz for the whole system. This constitutes a factor of approximately 25 in resonance frequency and a factor of 625 in stiffness and, hence, noise immunity.

Electronics↗
PubMed2004

Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization.

Tendons are composed of collagen and other molecules in a highly organized hierarchical assembly, leading to extraordinary mechanical properties. To probe the cross-links on the lower level of organization, we used a cantilever to pull substructures out of the assembly. Advanced force probe technology, using small cantilevers (length <20 microm), improved the force resolution into the sub-10 pN range. In the force versus extension curves, we found an exponential increase in force and two different periodic rupture events, one with strong bonds (jumps in force of several hundred pN) with a periodicity of 78 nm and one with weak bonds (jumps in force of <7 pN) with a periodicity of 22 nm. We demonstrate a good correlation between the measured mechanical behavior of collagen fibers and their appearance in the micrographs taken with the atomic force microscope.

Animals↗
PubMed2003

Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy.

Collagen type I displays a typical banding periodicity of 67 nm when visualized by atomic force or transmission electron microscopy imaging. We have investigated collagen fibers extracted from rat tail tendons using atomic force microscopy, under different ionic and pH conditions. The majority of the fibers reproduce the typical wavy structure with 67 nm spacing and a height difference between the peak and the grooves of at least 5 nm. However, we were also able to individuate two other banding patterns with 23+/-2 nm and 210+/-15 nm periodicities. The small pattern showed height differences of about 2 nm, whereas the large pattern seems to be a superposition of the 67 nm periodicity showing height differences of about 20 nm. Furthermore, we could show that at pH values of 3 and below the fibril structure gets dissolved whereas high concentrations of NaCl and CaCl(2) could prevent this effect.

Animals↗
PubMed2003

Evidence that collagen fibrils in tendons are inhomogeneously structured in a tubelike manner.

The standard model for the structure of collagen in tendon is an ascending hierarchy of bundling. Collagen triple helices bundle into microfibrils, microfibrils bundle into subfibrils, and subfibrils bundle into fibrils, the basic structural unit of tendon. This model, developed primarily on the basis of x-ray diffraction results, is necessarily vague about the cross-sectional organization of fibrils and has led to the widespread assumption of laterally homogeneous closepacking. This assumption is inconsistent with data presented here. Using atomic force microscopy and micromanipulation, we observe how collagen fibrils from tendons behave mechanically as tubes. We conclude that the collagen fibril is an inhomogeneous structure composed of a relatively hard shell and a softer, less dense core.

Animals↗