scholarly journals Nano-mechanical properties of individual mineralized collagen fibrils from bone tissue

2010 ◽  
Vol 8 (57) ◽  
pp. 500-505 ◽  
Author(s):  
Fei Hang ◽  
Asa H. Barber

Mineralized collagen fibrils (MCFs) are distinct building blocks for bone material and perform an important mechanical function. A novel experimental technique using combined atomic force microscopy and scanning electron microscopy is used to manipulate and measure the mechanical properties of individual MCFs from antler, which is a representative bone tissue. The recorded stress–strain response of individual MCFs under tension shows an initial linear deformation region for all fibrils, followed by inhomogeneous deformation above a critical strain. This inhomogeneous deformation is indicative of fibrils exhibiting either yield or strain hardening and suggests possible mineral compositional changes within each fibril. A phenomenological model is used to describe the fibril nano-mechanical behaviour.

2010 ◽  
Vol 1274 ◽  
Author(s):  
Fei Hang ◽  
Asa H Barber

AbstractAntler is an extraordinary bone tissue that displays significant overall toughness when compared to other bone materials. The origin of this toughness is due to the complex interaction between the nanoscale constituents as well as structural hierarchy in the antler material. Of particular interest is the mechanical performance of the interface between the collagen fibrils and considerably smaller volume of non-collagenous protein (NCP) between these fibrils. This paper directly examines the mechanical properties of isolated volumes of antler using combined in situ atomic force microscopy (AFM)-scanning electron microscopy (SEM) experiments. The antler material at the nanoscale is approximated to a fiber reinforced composite, with composite theory used to evaluate the interfacial shear stresses generated between the individual collagen fibrils and NCP during mechanical loading.


2010 ◽  
Vol 1274 ◽  
Author(s):  
Asa H Barber ◽  
Ines Jimenez-Palomar

AbstractBone is a complex material with structural features varying over many different length scales. Lamellae in bone are discrete units of collagen fibril arrays that are the dominant structural feature at length scales of a few microns. The mechanical properties of bone are importantly dependent on the synergy between the lamellae and structural features at other length scales. However, the mechanical properties at this micron level will be indicative of the bone material itself and ignores the structural and geometric organizations prevalent at larger length scales. The isolation of volumes of bone at the lamellar level requires precision cutting methodology and this paper exploits Focused Ion Beam (FIB) methods to mill small cantilever beams from bulk bone material. Importantly, FIB milling can only be performed in a relatively high vacuum environment. Atomic Force Microscopy (AFM) mechanical tests are therefore performed in two environments, high vacuum and air in order to assess the effects of vacuum on bone beam mechanical behaviour. Our results indicate that little difference in the bone beam elastic modulus is found from bending experiments at deflections up to 100nm in different environments.


2009 ◽  
Vol 1187 ◽  
Author(s):  
Fei Hang ◽  
Dun Lu ◽  
Asa H Barber

AbstractA technique combining both atomic force microscopy (AFM) and scanning electron microscopy (SEM) is used to evaluate the mechanical properties of individual collagen fibrils from the fractured surface of antler. SEM is used to locate individual mineralized collagen fibrils and allow visualization of the attachment of these fibrils to the end of an AFM probe. Tensile testing of individual collagen fibril to failure was performed using the AFM with resultant stress-strain curves obtained. Tensile strengths of up to 0.18GPa are found for some individual collagen fibrils, indicating the presence of mineral in improving mechanical performance. Consideration of the SEM operating parameters indicates that the amount of time the sample is within the SEM vacuum can affect the resultant mechanical behavior of individual fibrils.


2005 ◽  
Vol 127 (3) ◽  
pp. 383-390 ◽  
Author(s):  
Ozan Akkus

Mineralized collagen fibrils are the basic building blocks of bone tissue at the supramolecular level. Several disease states, manipulation of the expression of specific proteins involved in biomineralization, and treatment with different agents alter the extent of mineralization as well as the morphology of mineral crystals which in turn affect the mechanical function of bone tissue. An experimental assessment of mineralized fibers’ mechanical properties is challenged by their small size, leaving analytical and computational models as a viable alternative for investigation of the fibril-level mechanical properties. In the current study the variation of the elastic stiffness tensor of mineralized collagen fibrils with changing mineral volume fraction and mineral aspect ratios was predicted via a micromechanical model. The partitioning of applied stresses between mineral and collagen phases is also predicted for normal and shear loading of fibrils. Model predictions resulted in transversely isotropic collagen fibrils in which the modulus along the longer axis of the fibril was the greatest. All the elastic moduli increased with increasing mineral volume fraction whereas Poisson’s ratios decreased with the exception of ν12(=ν21). The partitioning of applied stresses were such that the stresses acting on mineral crystals were about 1.5, 15, and 3 times greater than collagen stresses when fibrils were loaded transversely, longitudinally, and in shear, respectively. In the overall the predictions were such that: (a) greatest modulus along longer axis; (b) the greatest mineral/collagen stress ratio along the longer axis of collagen fibers (i.e., greatest relief of stresses acting on collagen); and (c) minimal lateral contraction when fibers are loaded along the longer axis. Overall, the pattern of mineralization as put forth in this model predicts a superior mechanical function along the longer axis of collagen fibers, the direction which is more likely to experience greater stresses.


2000 ◽  
Vol 39 (Part 1, No. 6B) ◽  
pp. 3711-3716 ◽  
Author(s):  
Hatsuki Shiga ◽  
Yukako Yamane ◽  
Etsuro Ito ◽  
Kazuhiro Abe ◽  
Kazushige Kawabata ◽  
...  

Coatings ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 652
Author(s):  
Divine Sebastian ◽  
Chun-Wei Yao ◽  
Lutfun Nipa ◽  
Ian Lian ◽  
Gary Twu

In this work, a mechanically durable anticorrosion superhydrophobic coating is developed using a nanocomposite coating solution composed of silica nanoparticles and epoxy resin. The nanocomposite coating developed was tested for its superhydrophobic behavior using goniometry; surface morphology using scanning electron microscopy and atomic force microscopy; elemental composition using energy dispersive X-ray spectroscopy; corrosion resistance using atomic force microscopy; and potentiodynamic polarization measurements. The nanocomposite coating possesses hierarchical micro/nanostructures, according to the scanning electron microscopy images, and the presence of such structures was further confirmed by the atomic force microscopy images. The developed nanocomposite coating was found to be highly superhydrophobic as well as corrosion resistant, according to the results from static contact angle measurement and potentiodynamic polarization measurement, respectively. The abrasion resistance and mechanical durability of the nanocomposite coating were studied by abrasion tests, and the mechanical properties such as reduced modulus and Berkovich hardness were evaluated with the aid of nanoindentation tests.


Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1661
Author(s):  
Katarzyna Adamiak ◽  
Katarzyna Lewandowska ◽  
Alina Sionkowska

Collagen films are widely used as adhesives in medicine and cosmetology. However, its properties require modification. In this work, the influence of salicin on the properties of collagen solution and films was studied. Collagen was extracted from silver carp skin. The rheological properties of collagen solutions with and without salicin were characterized by steady shear tests. Thin collagen films were prepared by solvent evaporation. The structure of films was researched using infrared spectroscopy. The surface properties of films were investigated using Atomic Force Microscopy (AFM). Mechanical properties were measured as well. It was found that the addition of salicin modified the roughness of collagen films and their mechanical and rheological properties. The above-mentioned parameters are very important in potential applications of collagen films containing salicin.


2018 ◽  
Vol 114 (3) ◽  
pp. 513a
Author(s):  
Yuri M. Efremov ◽  
Mirian Velay-Lizancos ◽  
Daniel M. Suter ◽  
Pablo D. Zavattieri ◽  
Arvind Raman

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