Bone Micro- and Nanomechanics

Collins, Caitlyn J.; Andriotis, Orestis G.; Nedelkovski, Vedran; Frank, Martin; Katsamenis, Orestis L.; Thurner, Philipp J.

doi:10.1016/b978-0-12-801238-3.99937-9

Cited by 8 publications

(13 citation statements)

References 174 publications

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“…In native collagen, rope-like collagen molecules spontaneously assemble to form a three-dimensional crystalline lattice. As mentioned above, collagen fibrils are formed, in which the molecules are quasi-hexagonally packed and super-twisted in a right-handed structure along the longitudinal axis of the fibril ( Collins et al, 2019 ). Interestingly, the super-twisted structure of the fibrils is maintained also through the non-helical telopeptide regions ( Shoulders and Raines, 2009 ).…”

Section: Hierarchical Structure Of Type I Collagen and Related Bioactivitymentioning

confidence: 99%

“…Within the final crystalline lattice, water molecules surround each triple helix, forming a cylinder of hydration that contributes to stabilize the molecular structure ( Collins et al, 2019 ; Terzi et al, 2020 ). In addition to this “bound” water, free water is also found in the intra-fibrillar spaces.…”

Section: Hierarchical Structure Of Type I Collagen and Related Bioactivitymentioning

confidence: 99%

“…Interestingly, the super-twisted structure of the fibrils is maintained also through the non-helical telopeptide regions (Shoulders and Raines, 2009). Based on the X-ray diffraction patterns of native collagen, Orgel et al (2006) proposed a "microfibril" structural model having a triclinic unit cell formed by parts of five different collagen molecules (Collins et al, 2019). This is quite consistent with the simplified microfibril model previously proposed by Hodge and Petruska (1963), who envisaged a bidimensional stack of five collagen molecules aligned parallel to one another with a staggering of about 67 nm (Figure 2).…”

Section: Quaternary Structurementioning

confidence: 99%

“…Therefore, while telopeptides might not be essential for fibrillogenesis, they are fundamental to strengthen the fibrils via the formation of crosslinks (Shoulders and Raines, 2009). Within the final crystalline lattice, water molecules surround each triple helix, forming a cylinder of hydration that contributes to stabilize the molecular structure (Collins et al, 2019;Terzi et al, 2020). In addition to this "bound" water, free water is also found in the intra-fibrillar spaces.…”

Section: Quaternary Structurementioning

confidence: 99%

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Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Salvatore

Gallo

Natali

et al. 2021

Front. Bioeng. Biotechnol.

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Biological materials found in living organisms, many of which are proteins, feature a complex hierarchical organization. Type I collagen, a fibrous structural protein ubiquitous in the mammalian body, provides a striking example of such a hierarchical material, with peculiar architectural features ranging from the amino acid sequence at the nanoscale (primary structure) up to the assembly of fibrils (quaternary structure) and fibers, with lengths of the order of microns. Collagen plays a dominant role in maintaining the biological and structural integrity of various tissues and organs, such as bone, skin, tendons, blood vessels, and cartilage. Thus, “artificial” collagen-based fibrous assemblies, endowed with appropriate structural properties, represent ideal substrates for the development of devices for tissue engineering applications. In recent years, with the ultimate goal of developing three-dimensional scaffolds with optimal bioactivity able to promote both regeneration and functional recovery of a damaged tissue, numerous studies focused on the capability to finely modulate the scaffold architecture at the microscale and the nanoscale in order to closely mimic the hierarchical features of the extracellular matrix and, in particular, the natural patterning of collagen. All of these studies clearly show that the accurate characterization of the collagen structure at the submolecular and supramolecular levels is pivotal to the understanding of the relationships between the nanostructural/microstructural properties of the fabricated scaffold and its macroscopic performance. Several studies also demonstrate that the selected processing, including any crosslinking and/or sterilization treatments, can strongly affect the architecture of collagen at various length scales. The aim of this review is to highlight the most recent findings on the development of collagen-based scaffolds with optimized properties for tissue engineering. The optimization of the scaffolds is particularly related to the modulation of the collagen architecture, which, in turn, impacts on the achieved bioactivity.

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Section: Hierarchical Structure Of Type I Collagen and Related Bioactivitymentioning

confidence: 99%

Section: Hierarchical Structure Of Type I Collagen and Related Bioactivitymentioning

confidence: 99%

Section: Quaternary Structurementioning

confidence: 99%

Section: Quaternary Structurementioning

confidence: 99%

See 2 more Smart Citations

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Salvatore

Gallo

Natali

et al. 2021

Front. Bioeng. Biotechnol.

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“…It possesses a special hierarchical structure that has been deeply studied both with experimental and modeling tools across different length scales [4][5][6][7][8][9][10][11][12] . Among them, the molecular scale is the observation level that is still open to new research avenues, since the material composition and its microstructural factors determine bone properties and dynamic behavior [13][14][15] . Bone presents a staggered periodicity length, derived from pure collagenous tissues, called D-period of ≈ 67 nm, which is composed of two parts named overlap and gap regions 10,16 .…”

Section: Introductionmentioning

confidence: 99%

Molecular origin of viscoelasticity in mineralized collagen fibrils

et al. 2021

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The Role of the Extrafibrillar Volume on the Mechanical Properties of Molecular Models of Mineralized Bone Microfibrils

Alcântara

Felix

Galvão

et al. 2022

ACS Biomater. Sci. Eng.

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Bones are responsible for body support, structure, motion, and several other functions that enable and facilitate life for many different animal species. They exhibit a complex network of distinct physical structures and mechanical properties, which ultimately depend on the fraction of their primary constituents at the molecular scale. However, the relationship between structure and mechanical properties in bones are still not fully understood. Here, we investigate structural and mechanical properties of all-atom bone molecular models composed of type-I collagen, hydroxyapatite (HA), and water by means of fully atomistic molecular dynamics simulations. Our models encompass an extrafibrillar volume (EFV) and consider mineral content in both the EFV and intrafibrillar volume (IFV), consistent with experimental observations. We investigate solvation structures and elastic properties of bone microfibril models with different degrees of mineralization, ranging from highly mineralized to weakly mineralized and nonmineralized models. We find that the local tetrahedral order of water is lost in similar ways in the EFV and IFV regions for all HA containing models, as calcium and phosphate ions are strongly coordinated with water molecules. We also subject our models to tensile loads and analyze the spatial stress distribution over the nanostructure of the material. Our results show that both mineral and water contents accumulate significantly higher stress levels, most notably in the EFV, thus revealing that this region, which has been only recently incorporated in all-atom molecular models, is fundamental for studying the mechanical properties of bones at the nanoscale. Furthermore, our results corroborate the well-established finding that high mineral content makes bone stiffer.

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Bone Micro- and Nanomechanics

Cited by 8 publications

References 174 publications

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Molecular origin of viscoelasticity in mineralized collagen fibrils

The Role of the Extrafibrillar Volume on the Mechanical Properties of Molecular Models of Mineralized Bone Microfibrils

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