Stress Dependent Collagen Fibril Diameter Distribution in Human Aortic Valves

2007 ◽  
Author(s):  
Angelique Balguid ◽  
Anita Mol ◽  
Niels Driessen ◽  
Carlijn Bouten ◽  
Frank Baaijens
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Diameter Distribution ◽  
Connective Tissues ◽  
Aortic Valves ◽  
Cross Links ◽  
Fibril Morphology ◽  
Stress Dependent ◽  
Collagenous Tissues ◽  
Fibril Diameter

The mechanical properties of collagenous tissues are known to depend on a wide variety of factors, such as the type of tissue and the composition of its extracellular matrix. Relating mechanical roles to individual matrix components in such a complex system is difficult, if not impossible. However, as collagen is the main load bearing component in connective tissues, the relation between collagen and tissue biomechanics has been studied extensively in various types of tissues. The type of collagen, the amount and type of inter- and intramolecular covalent cross-links and collagen fibril morphology are involved in the tissues mechanical behavior (Beekman et al., 1997; Parry et al., 1978; Avery and Bailey, 2005). From literature it is known that the the collagen fibril diameter distribution can be directly related to the mechanical properties of the tissue. In particular, the diameter distribution of collagen fibrils is largely determined by the tissues requirement for tensile strength and elasticity (Parry et al., 1978).

A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relation between fibril size distribution and mechanical properties

1978 ◽  
Vol 203 (1152) ◽  
pp. 305-321 ◽  
Keyword(s):  
Mechanical Properties ◽  
Tensile Strength ◽  
Size Distribution ◽  
Collagen Fibril ◽  
Average Diameter ◽  
Collagen Fibrils ◽  
Diameter Distribution ◽  
Connective Tissues ◽  
Fibril Diameter ◽  
Covalent Crosslinks

Data on the distribution of collagen fibril diameters in various connective tissues have been collected and analysed for common features. The diameter distributions of the collagen fibrils at birth and in the foetal stages of development are unimodal, whereas at maturity the mass-average diameter of the collagen fibrils is generally larger than at birth and the distributions of fibril sizes may be either unimodal or bimodal depending on the tissue. At senescence, few data are available but in most instances both the mean and mass-average diameters of the collagen fibrils are smaller than those at maturity and the fibril distributions are mainly bimodal. The division between tissues showing unimodal or bimodal fibril distributions at maturity does not simply relate to the type I collagen/type II collagen classification, to the distinction between orientated and unorientated material or indeed directly to the levels of stress and strain encountered by the tissue. However, there may prove to be a relation between a bimodal fibril diameter distribution at maturity and the maintenance over long periods of time of either high stress in stretched tissues or low stress in compressed tissues. It has also been noted that the width of the collagen fibril diameter distribution at birth differs between altricious and precocious animals. The ultimate tensile strength of a connective tissue and the mass-average diameter of the constituent collagen fibrils have been shown to have a positive correlation. Further, the form of the collagen fibril diameter distribution can be directly related to the mechanical properties of the tissue. In particular, it is postulated that the size distribution of the collagen fibrils is largely determined by two factors. First, if the tissue is primarily designed to have high tensile strength, then an increase in the diameter of the collagen fibrils will parallel an increase in the potential density of intrafibrillar covalent crosslinks. Consequently large collagen fibrils are predicted to have a greater tensile strength than small fibrils. Secondly, if the tissue is designed to be elastic and hence withstand creep, then a reduction in the diameter of the collagen fibrils will effectively increase the surface area per unit mass of the fibrils thus enhancing the probability of interfibrillar non-covalent crosslinks between the collagen fibrils and the components of the matrix. The idealized description given may indicate how the mechanical properties of a tissue may be interpreted in terms of the collagen fibril diameter distribution.

scholarly journals Pilot study on the effects of preservatives on corneal collagen parameters measured by small angle X-ray scattering analysis

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Susyn Joan Kelly ◽  
Lizette duPlessis ◽  
John Soley ◽  
Frazer Noble ◽  
Hannah Carolyn Wells ◽  
...  
Keyword(s):  
Small Angle ◽  
Collagen Fibril ◽  
Diameter Distribution ◽  
X Ray ◽  
X Ray Scattering ◽  
Saxs Analysis ◽  
Triton X ◽  
Fibril Diameter ◽  
Corneal Collagen ◽  
Ray Scattering

Abstract Objective Small angle X-ray scattering (SAXS) analysis is a sensitive way of determining the ultrastructure of collagen in tissues. Little is known about how parameters measured by SAXS are affected by preservatives commonly used to prevent autolysis. We determined the effects of formalin, glutaraldehyde, Triton X and saline on measurements of fibril diameter, fibril diameter distribution, and D-spacing of corneal collagen using SAXS analysis. Results Compared to sections of sheep and cats’ corneas stored frozen as controls, those preserved in 5% glutaraldehyde and 10% formalin had significantly larger mean collagen fibril diameters, increased fibril diameter distribution and decreased D-spacing. Sections of corneas preserved in Triton X had significantly increased collagen fibril diameters and decreased fibril diameter distribution. Those preserved in 0.9% saline had significantly increased mean collagen fibril diameters and decreased diameter distributions. Subjectively, the corneas preserved in 5% glutaraldehyde and 10% formalin maintained their transparency but those in Triton X and 0.9% saline became opaque. Subjective morphological assessment of transmission electron microscope images of corneas supported the SAXS data. Workers using SAXS analysis to characterize collagen should be alerted to changes that can be introduced by common preservatives in which their samples may have been stored.

Ageing Changes in the Tensile Properties of Tendons: Influence of Collagen Fibril Volume Fraction

2008 ◽  
Vol 130 (2) ◽  
Author(s):  
K. L. Goh ◽  
D. F. Holmes ◽  
H.-Y. Lu ◽  
S. Richardson ◽  
K. E. Kadler ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Volume Fraction ◽  
Area Fraction ◽  
Sectional Area ◽  
Cross Sectional ◽  
P Values ◽  
Age Related ◽  
Fibril Diameter ◽  
Age Related Changes

Connective tissues are biological composites comprising of collagen fibrils embedded in (and reinforcing) the hydrated proteoglycan-rich (PG) gel within the extracellular matrices (ECMs). Age-related changes to the mechanical properties of tissues are often associated with changes to the structure of the ECM, namely, fibril diameter. However, quantitative attempts to correlate fibril diameter to mechanical properties have yielded inconclusive evidence. Here, we described a novel approach that was based on the rule of mixtures for fiber composites to evaluate the dependence of age-related changes in tendon tensile strength (σ) and stiffness (E) on the collagen fibril cross-sectional area fraction (ρ), which is related to the fibril volume fraction. Tail tendons from C57BL6 mice from age groups 1.6–35.3months old were stretched to failure to determine σ and E. Parallel measurements of ρ as a function of age were made using transmission electron microscopy. Mathematical models (rule of mixtures) of fibrils reinforcing a PG gel in tendons were used to investigate the influence of ρ on ageing changes in σ and E. The magnitudes of σ, E, and ρ increased rapidly from 1.6monthsto4.0months (P-values <0.05) before reaching a constant (age independent) from 4.0monthsto29.0months (P-values >0.05); this trend continued for E and ρ (P-values >0.05) from 29.0monthsto35.3months, but not for σ, which decreased gradually (P-values <0.05). Linear regression analysis revealed that age-related changes in σ and E correlated positively to ρ (P-values <0.05). Collagen fibril cross-sectional area fraction ρ is a significant predictor of ageing changes in σ and E in the tail tendons of C57BL6 mice.

Growth and development of collagen fibrils in immature tissues from rat and sheep

1981 ◽  
Vol 212 (1186) ◽  
pp. 85-92 ◽  
Keyword(s):  
Electron Microscope ◽  
Transmission Electron Microscope ◽  
Collagen Fibril ◽  
Growth And Development ◽  
Collagen Fibrils ◽  
Diameter Distribution ◽  
Rat Tissues ◽  
Transmission Electron ◽  
The Mean ◽  
Fibril Diameter

The collagen fibril diameter distribution of four immature tissues from both rat and sheep have been determined from transverse sections observed in the transmission electron microscope. In many instances before birth, the form of the distribution for the tissues is both unimodal and sharp and the mean diameters of the distributions lie close to a multiple of 80 Å. For some tissues, the collagen fibril diameter distributions may be resolved into a number of components, each of which represents a population of fibrils with a diameter close to a multiple of 80 Å (8 nm). These data confirm and extend previous observations by the authors that small collagen fibrils all have diameters that are multiples of about 80 Å and that the fibril growth occurs by the accretion of 80 Å units. The form of the collagen fibril diameter distribution at birth is broad for the sheep tissues but narrow for the rat tissues, thus confirming that the range of fibril diameters at this stage of life reflects the differing degree of development of precocious and altricious animals.

scholarly journals Nanostructural and mechanical changes in the sclera following proteoglycan depletion

2018 ◽  
Vol 2 (2) ◽  
pp. 14-17
Author(s):  
Zhuola Zhuola ◽  
Steve Barrett ◽  
Yalda Ashraf Kharaz ◽  
Riaz Akhtar
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Enzymatic Degradation ◽  
Ocular Tissues ◽  
Force Microscopy ◽  
Nanomechanical Properties ◽  
Atomic Force ◽  
Fibril Morphology

The mechanical properties of ocular tissues, such as the sclera, have a major impact on healthy eye function, and are governed by the properties and composition of the microstructural components. For example, biomechanical degradation associated with myopia occurs alongside a reduction of proteoglycans (PGs). In this study, the role of PG degradation in the nanomechanical properties of the porcine sclera is explored. In-vitro enzymatic degradation of PGs was conducted with α-amylase and chondroitinase ABC enzymes. Collagen fibril morphology and nanomechanical stiffness were measured with atomic force microscopy (AFM). The elastic modulus of the tissue was reduced in all enzyme-treated samples relative to controls. In addition, collagen fibril organization was disrupted by PG depletion. Our data demonstrate that PGs play an important role in determining not only the mechanical properties at these length scales, but also collagen fibril arrangement.

scholarly journals Effects of Preservatives on Corneal Collagen Parameters Measured by Small Angle X-Ray Scattering Analysis

2020 ◽  
Author(s):  
Susyn Kelly ◽  
Lizette duPlessis ◽  
John Soley ◽  
Frazer Noble ◽  
Hannah Carolyn Wells ◽  
...  
Keyword(s):  
Small Angle ◽  
Collagen Fibril ◽  
Diameter Distribution ◽  
X Ray ◽  
X Ray Scattering ◽  
Saxs Analysis ◽  
Triton X ◽  
Fibril Diameter ◽  
Corneal Collagen ◽  
Ray Scattering

Abstract Objective: Small angle X-ray scattering (SAXS) analysis is a sensitive method for determining the ultrastructure of collagen in various tissues. Little is known about how parameters measured by SAXS are affected by preservatives, commonly used to prevent autolysis and strengthen sample tissues. We determined the effects of formalin, glutaraldehyde, Triton X and saline on measurements of fibril diameter, fibril diameter distribution, and D-spacing of corneal collagen using SAXS analysis. Results: Compared to control sheep and cats’ corneas, frozen at -80 °C, those preserved in 5% glutaraldehyde and 10% formalin had significantly larger mean collagen fibril diameters, increased fibril diameter distribution and decreased D-spacing. Corneas preserved in Triton X had significantly increased collagen fibril diameters and decreased fibril diameter distribution. Corneas preserved in 0.9% saline had significantly increased mean collagen fibril diameters and decreased diameter distributions. Subjectively, the corneas preserved in 5% glutaraldehyde and 10% formalin maintained their transparency but those in Triton X and 0.9% saline became opaque. Subjective morphological assessment of transmission electron microscope images of corneas supported the SAXS data. Workers using SAXS analysis to characterize collagen should be alerted to changes that can be introduced by common preservatives in which their samples may have been stored.

Obesity Affects Collagen Fibril Diameter and Mechanical Properties of Tendons in Zucker Rats

2010 ◽  
Vol 51 (3) ◽  
pp. 171-178 ◽  
Author(s):  
Adriano Biancalana ◽  
LícioA. Veloso ◽  
Laurecir Gomes
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Zucker Rats ◽  
Fibril Diameter
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