Production of a Novel, Self-Assembled, Collagenous Matrix Mimicking the Hierarchical Structure of Native Aligned Connective Tissue

1995 ◽  
Vol 414 ◽  
Author(s):  
G. D. Pins ◽  
D. L. Christiansen ◽  
R. Patel ◽  
F. H. Silver
Keyword(s):  
Self Assembly ◽  
Collagen Fiber ◽  
Type I Collagen ◽  
Tensile Tests ◽  
Fiber Formation ◽  
Morphological Properties ◽  
Uniaxial Tensile ◽  
Type I ◽  
Native Collagen

AbstractThe primary goal of the biomaterials scientist and tissue engineer is to create a biocompatible implant which mimics the mechanical and morphological properties of the tissue being replaced. In vitro experimentation has documented the propensity of soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native collagen fiber. Our laboratory has further investigated in vitro self-assembly by incorporating several of the “natural” processes into a multi-step fiber formation procedure which generates macroscopic collagen fiber from its molecular constituents. Results of uniaxial tensile tests and ultrastructural analyses indicate that these coextruded and stretched collagen fibers have mechanical properties and fibrillar substructure comparable to that observed in native collagen fiber.

scholarly journals Fourier transform infrared conformational investigation of type I collagen aged by in vitro induced dehydration and non-enzymatic glycation treatments

2017 ◽  
Vol 90 (1) ◽  
Author(s):  
Maria Grazia Bridelli ◽  
Chiaramaria Stani ◽  
Roberta Bedotti
Keyword(s):  
Fourier Transform ◽  
Protein Structure ◽  
Conformational Changes ◽  
Self Assembly ◽  
Type I Collagen ◽  
Protein Secondary Structure ◽  
Fourier Transform Infrared ◽  
Type I ◽  
Absorption Bands

The two main ageing-inducing events in the collagenous tissues are the water loss and the formation of intermolecular crosslinks based on the reaction of collagen with matrix carbohydrates, following a mechanism known as non-enzymatic-glycation. With the aim to mimic the two deleterious processes for the protein structure, rat-tail collagen was submitted to hydration changes and allowed to interact with two sugars characterized by different reducing properties, D-glucose and D-ribose. Fourier transform infrared (FTIR) spectroscopy was employed to investigate the conformational changes induced in the protein by the two treatments by analyzing the subsequent spectra modifications. FTIR spectra monitored: i) the amplitude and position changes of the two characteristic absorption bands OH stretching and Amide I, in dependence on the humidity level: a significant hysteresis effect in the ν(OH) band (ν~3400 cm–1) amplitude of the protein dehydrated and then rehydrated to the initial relative humidity (aw=0.92- 0.06) may be related to the enhancement of the β-sheet fraction in the protein structure as revealed by the parallel modification in the Amide I band (ν~1650 cm–1); ii) the area of the carbohydrate double band peaking at 1080 cm–1 and 1031 cm–1, associated to the accumulation of the glycation products, depending on the sugar concentration and incubation time. The association of both sugars to collagen only minimally affects the protein secondary structure as revealed by Amide I band Gaussian analysis. The whole set of results suggests hints to hypothesize a self-assembly model for collagen molecules induced by ageing.

Microaligned collagen matrices by hydrodynamic focusing: controlling the pH-induced self-assembly

2005 ◽  
Vol 898 ◽  
Author(s):  
Sarah Köester ◽  
Jennie B Leach ◽  
Thomas Pfohl ◽  
Joyce Y Wong
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Polarized Light ◽  
Type I ◽  
Hydrodynamic Focusing ◽  
Microfluidic Mixing ◽  
Ph Gradients ◽  
The Hierarchical Structure ◽  
Local Ph

AbstractThe hierarchical structure of type I collagen fibrils is a key contributor to the mechanical properties of the extracellular matrix (ECM). It is known that the process of in vitro fibrillogenesis strongly depends on the pH of the collagen solution. To date, there are few methods available for precisely controlling and investigating the dependence of collagen fibril assembly on the local pH. The objective of this work was to create highly defined pH gradients to systematically determine the effects of local pH on microscale collagen fibrillogenesis and alignment. We use a microfluidic mixing device to create a diffusion controlled pH gradient, which in turn initiates the self-assembly and concurrent flow-alignment of soluble collagen. Finite element method simulations of the hydrodynamic and diffusive phenomena are used to calculate the local concentrations of the components involved in the reaction. We develop a model to analytically calculate the local pH in the microfluidic device from these concentrations. A comparison with the experimental results from polarized light microscopy are in good agreement with the simulations.

Discontinuous change of the activation energy on Type I collagen in vitro self-assembly.

1999 ◽  
Vol 39 (supplement) ◽  
pp. S165
Author(s):  
I. Someki ◽  
T. Ebihara ◽  
E. Adachi ◽  
S. Hattori ◽  
S. Irie
Keyword(s):  
Activation Energy ◽  
Self Assembly ◽  
Type I Collagen ◽  
Type I ◽  
Discontinuous Change

Turbidimetric and morphological studies of type I collagen fibre self assembly in vitro and the influence of fibronectin

1985 ◽  
Vol 7 (3) ◽  
pp. 135-140 ◽  
Author(s):  
Jane L. Brokaw ◽  
Charles J. Doillon ◽  
Rita A. Hahn ◽  
David E. Birk ◽  
Richard A. Berg ◽  
...  
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Collagen Fibre ◽  
Type I ◽  
Morphological Studies

In Vitro Reconstruction of Hybrid Arterial Media with Molecular and Cellular Orientations

1994 ◽  
Vol 3 (6) ◽  
pp. 537-545 ◽  
Author(s):  
Keiichi Kanda ◽  
Takehisa Matsuda
Keyword(s):  
Collagen Fiber ◽  
Type I Collagen ◽  
Dynamic Stress ◽  
Collagen Gel ◽  
Fiber Bundles ◽  
Outer Diameter ◽  
Type I ◽  
Silicone Tube ◽  
Aortic Media

A hybrid medial tissue composed of a type I collagen gel, into which smooth muscle cells (SMCs) derived from bovine aortic media were 3-dimensionally (3D) embedded, was constructed around an elastomeric silicone tube (outer diameter: 8 mm). Subsequently, hybrid tissues thus prepared were subjected to three modes of mechanical stimulation in the medium: one was subjected to flotation with no disturbance (isotonic control), the second was kept isometrically (static stress) and the third was subjected to continuous periodic stretch by inflation of the embedded silicone tube which simulated arterial pulsation (dynamic stress, amplitude: 5% in inner diameter; frequency: 60 RPM). After a 5-day culture period, hybrid tissues were morphologically investigated. In control gels, polygonal SMCs and extracellular collagen fiber bundles were randomly oriented. On the other hand, upon static or dynamic stress loading, bipolar spindle-shaped SMCs and dense collagen fiber bundles were aligned circumferentially around the silicone tube, which proceeded with time. The orientations of SMCs and collagen fibers were more prominent in dynamically stressed hybrid tissues than those in statically stressed ones. The pulsatile stress-loaded hybrid medial tissue mimicked the media of native muscular arteries in terms of cellular and molecular orientations.

In vitro crystal growth of octacalcium phosphate on type I collagen fiber

1994 ◽  
Vol 137 (3-4) ◽  
pp. 553-560 ◽  
Author(s):  
Mayumi Iijima ◽  
Yutaka Moriwaki ◽  
Yoshinori Kuboki
Keyword(s):  
Crystal Growth ◽  
Collagen Fiber ◽  
Type I Collagen ◽  
Octacalcium Phosphate ◽  
Type I

scholarly journals Marangoni flows drive the alignment of fibrillar cell-laden hydrogels

2020 ◽  
Vol 6 (24) ◽  
pp. eaaz7748 ◽  
Author(s):  
Bryan A. Nerger ◽  
P.-T. Brun ◽  
Celeste M. Nelson
Keyword(s):  
Self Assembly ◽  
Collagen Fiber ◽  
Type I Collagen ◽  
Type I ◽  
Sessile Droplet ◽  
Biomimetic Materials ◽  
Fiber Assembly ◽  
Self Assembling ◽  
Surrounding Environment ◽  
Marangoni Flows

When a sessile droplet containing a solute in a volatile solvent evaporates, flow in the droplet can transport and assemble solute particles into complex patterns. Transport in evaporating sessile droplets has largely been examined in solvents that undergo complete evaporation. Here, we demonstrate that flow in evaporating aqueous sessile droplets containing type I collagen—a self-assembling polymer—can be harnessed to engineer hydrated networks of aligned collagen fibers. We find that Marangoni flows direct collagen fiber assembly over millimeter-scale areas in a manner that depends on the rate of self-assembly, the relative humidity of the surrounding environment, and the geometry of the droplet. Skeletal muscle cells that are incorporated into and cultured within these evaporating droplets collectively orient and subsequently differentiate into myotubes in response to aligned networks of collagen. Our findings demonstrate a simple, tunable, and high-throughput approach to engineer aligned fibrillar hydrogels and cell-laden biomimetic materials.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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