Atomic force microscopy of collagen structure in bone and dentine revealed by osteoclastic resorption

Bozec, Laurent; Groot, Jaco de; Odlyha, Marianne; Nicholls, Brian M.; Nesbitt, Stephen A.; Flanagan, Adrienne M.; Horton, Michael A.

doi:10.1016/j.ultramic.2005.06.021

Cited by 47 publications

(40 citation statements)

References 32 publications

(38 reference statements)

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“…Gaps were detected every 200-300 nm along these flat bundles which are also found in the collagen of natural bone [9]. D-periodic cross-striated collagen nanofibrils were detected in the AFM phase angle mapping images with an average D = 65 nm which has also been found in the AFM of natural bone [41].…”

Section: Discussionsupporting

confidence: 53%

Structural hierarchy of biomimetic materials for tissue engineered vascular and orthopedic grafts

et al. 2007

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Gelatine gels and gelatine/elastin gels have been prepared to be used in tissue engineered vascular grafts. Optical microscopy and AFM revealed that the gelatine formed nanofibrils as in soft collagen tissues. The gelatine/elastin gels were nanocomposites with flat elastin nanodomains embedded in the gelatine matrix mimicking the structure of the tunica media in arteries. Gelatine/"hydroxyapatite" nanocomposites were prepared with the in situ production of "hydroxyapatite" in solution. AFM revealed "hydroxyapatite" solid nanoparticles of about 20 nm size embedded in the gelatine matrix which formed a hierarchical structure similar to that of the collagen matrix in bone. The application of a magnetic field of 9.4 T resulted in the elongation and orientation of gelatine particles and orientation of gelatine microfibrils in a direction perpendicular to that of the magnetic field.3

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Section: Discussionsupporting

confidence: 53%

Structural hierarchy of biomimetic materials for tissue engineered vascular and orthopedic grafts

et al. 2007

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“…Collagen plays an important role in many biological tissues, including tendon, bone, teeth, and cartilage (6,7,13,15,19,21). Severe mechanical tensile loading of collagen is significant under many physiological conditions, as in joints and in bone (22, 23).…”

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confidence: 99%

Nature designs tough collagen: Explaining the nanostructure of collagen fibrils

Buehler

2006

Proc. Natl. Acad. Sci. U.S.A.

690

498

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Collagen is a protein material with superior mechanical properties. It consists of collagen fibrils composed of a staggered array of ultra-long tropocollagen (TC) molecules. Theoretical and molecular modeling suggests that this natural design of collagen fibrils maximizes the strength and provides large energy dissipation during deformation, thus creating a tough and robust material. We find that the mechanics of collagen fibrils can be understood quantitatively in terms of two critical molecular length scales S and R that characterize when (i) deformation changes from homogeneous intermolecular shear to propagation of slip pulses and when (ii) covalent bonds within TC molecules begin to fracture, leading to brittle-like failure. The ratio S͞R indicates which mechanism dominates deformation. Our modeling rigorously links the chemical properties of individual TC molecules to the macroscopic mechanical response of fibrils. The results help to explain why collagen fibers found in nature consist of TC molecules with lengths in the proximity of 300 nm and advance the understanding how collagen diseases that change intermolecular adhesion properties influence mechanical properties.deformation ͉ fracture ͉ mechanics ͉ tropocollagen ͉ length scale M aterials found in nature often feature hierarchical structures ranging from the atomistic and molecular scales to macroscopic scales (1-5). Many biological materials found in living organisms, often protein-based, feature a complex hierarchical design.Collagen, the most abundant protein on earth, is a fibrous structural protein with superior mechanical properties, and it provides an intriguing example of a hierarchical biological nanomaterial (4, 6-18). Collagen consists of tropocollagen (TC) molecules that have lengths of L Ϸ 280 nm and diameters of Ϸ1.5 nm, leading to an aspect ratio of Ϸ190 (6, 7, 9, 18-20). Staggered arrays of TC molecules form fibrils, which arrange to form collagen fibers (Fig. 1).Collagen plays an important role in many biological tissues, including tendon, bone, teeth, and cartilage (6,7,13,15,19,21). Severe mechanical tensile loading of collagen is significant under many physiological conditions, as in joints and in bone (22, 23). Despite significant research effort over the past couple of decades, the geometry and typical length scales found in collagen fibrils, the deformation mechanisms under mechanical load, and, in particular, the relationship between those mechanisms and collegen's molecular and intermolecular properties, are not well understood. Moreover, the limiting factors of the strength of collagen fibrils and the origins of toughness remain largely unknown.Some experimental efforts focused on the deformation mechanics of collagen fibril at nanoscale, including the characterization of changes of D-spacing and fibril orientation (18,20,24), analyses that featured x-ray diffraction (18) and synchrotron radiation experiments (19). Other experimental studies were focused on the averaged response of arrays of collagen fibrils, considering nan...

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“…Every 200-300 nm along the flat nanofibril bundles, there are gaps, which have also been detected in the collagen of natural bone [5]. The AFM angle phase mapping of Fig.3(a) shows evidence of D-periodic cross-striated collagen nanofibrils with an average D of 65 nm, which has also been detected in the AFM of natural bone [22]. Fig.4(a) shows "HA" nanoparticles of similar size but fewer as this is the gel with the lower ratio of "HA"/gelatine of 0.50 g/g, splitting the fibre bed in wider bundles of crosslinked gelatine nanofibrils of about 100 nm.…”

Section: Micro-and Nano-structure Of "Ha"/gelatine Gels and Foamsmentioning

confidence: 66%

Gelatine-Hydroxyapatite Nano-composites for Orthopaedic Applications

Vidyarthi¹,

Zhdan²,

Gravanis³

et al. 2008

AIP Conference Proceedings

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Abstract-This study focuses on the preparation and testing of hydroxyapatite-gelatine nanocomposite gels via a sol-gel route and in situ formation of hydroxyapatite (HA) type salts. Four types of gels and foams were prepared with Ca/P molar ratio of 0.43 and 0.86 and hydroxyapatite/gelatine weight ratio of 0.50 and 0.70. Crosslinking of gelatine chains was carried out in 1% glutaraldehyde and dynamic mechanical torsion tests were used to measure the viscoelastic properties of the gels and foams, optimize the crosslinking time and assess their mechanical performance. Optical and atomic force microscopy were used to investigate the micro-and nano-structure of the produced composites: in these studies, it was confirmed that the gels were nanocomposites with a nano-structure very similar to that of bone and several similarities in the microstructural features. The best foams incorporated dual pore size distribution.

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Atomic force microscopy of collagen structure in bone and dentine revealed by osteoclastic resorption

Cited by 47 publications

References 32 publications

Structural hierarchy of biomimetic materials for tissue engineered vascular and orthopedic grafts

Structural hierarchy of biomimetic materials for tissue engineered vascular and orthopedic grafts

Nature designs tough collagen: Explaining the nanostructure of collagen fibrils

Gelatine-Hydroxyapatite Nano-composites for Orthopaedic Applications

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