Mechanics of a two-fiber model with one nested fiber network, as applied to the collagen-fibrin system

Nedrelow, David S.; Bankwala, Danesh; Hyypio, Jeffrey D.; Lai, Victor K.; Barocas, Victor H.

doi:10.1016/j.actbio.2018.03.053

Cited by 10 publications

(10 citation statements)

References 48 publications

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“…Moreover, further observations indicated that when one of the proteins is present in a small amount only, it does not form a percolating network. This raised the hypothesis of an "island" model, where the more diluted protein tends to locally concentrate rather than being homogeneously dispersed in the other protein network ( Figure 5) [143]. Such a model was able to better reproduce experimental data in the low collagen and low fibrin composition domains.…”

Section: Type I Collagen-fibrin Mixed Hydrogels: Structure and Mechanmentioning

confidence: 97%

“…Typical protein concentrations used in these protocols range between 1 and 5 mg mL −1 . In most cases, 1:1 collagen:fibrin mixed hydrogels are prepared but several studies have explored a series of materials of intermediate concentrations [121,122,124,134,138,140,141,143].…”

Section: From Protein Mixturesmentioning

confidence: 99%

“…TEM is more adapted to study fibril structure but, surprisingly, it was very rarely used to characterize mixed collagen-fibrin materials [111,145]. Confocal imaging using fluorescently-labelled proteins or, in the case of collagen, second harmonic generation microscopy, can allow to visualize the two networks but at a higher scale [130,143]. Thus, in many cases, the structure of the mixed networks is deduced from their mechanical behavior.…”

Section: Type I Collagen-fibrin Mixed Hydrogels: Structure and Mechanmentioning

confidence: 99%

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Type I Collagen-Fibrin Mixed Hydrogels: Preparation, Properties and Biomedical Applications

Coradin

Wang

Law

et al. 2020

Gels

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Type I collagen and fibrin are two essential proteins in tissue regeneration and have been widely used for the design of biomaterials. While they both form hydrogels via fibrillogenesis, they have distinct biochemical features, structural properties and biological functions which make their combination of high interest. A number of protocols to obtain such mixed gels have been described in the literature that differ in the sequence of mixing/addition of the various reagents. Experimental and modelling studies have suggested that such co-gels consist of an interpenetrated structure where the two proteins networks have local interactions only. Evidences have been accumulated that immobilized cells respond not only to the overall structure of the co-gels but can also exhibit responses specific to each of the proteins. Among the many biomedical applications of such type I collagen-fibrin mixed gels, those requiring the co-culture of two cell types with distinct affinity for these proteins, such as vascularization of tissue engineering constructs, appear particularly promising.

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Section: Type I Collagen-fibrin Mixed Hydrogels: Structure and Mechanmentioning

confidence: 97%

Section: From Protein Mixturesmentioning

confidence: 99%

Section: Type I Collagen-fibrin Mixed Hydrogels: Structure and Mechanmentioning

confidence: 99%

See 1 more Smart Citation

Type I Collagen-Fibrin Mixed Hydrogels: Preparation, Properties and Biomedical Applications

Coradin

Wang

Law

et al. 2020

Gels

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“…co-dependent networks) model of collagen and fibrin materials. They partially explained mechanical properties obtained in this study in a second article using a model of non-percolating network in which islands of the diluted protein are embedded in the concentrated one 48 . Such conclusion is in total agreement with the structure observed in mix threads, with islands of fibrin inside the collagen matrix ( Fig.1.C.2).…”

Section: Mechanical Propertiesmentioning

confidence: 55%

Differential myoblast and tenoblast affinity to collagen, fibrin and mixed threads in the prospect of muscle-tendon junction modelisation

Rieu¹,

Rose²,

Taleb³

et al. 2020

Preprint

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The myotendinous junction transfers forces from muscle to tendon. As such, it must hold two tissues of completely different biological and cellular compositions as well as mechanical properties (kPa-MPa to MPa-GPa) and is subject to frequent stresses of high amplitude. This region remains a weak point of the muscle-tendon unit and is involved in frequent injuries. We here produce fibrin (40 mg/mL, E0 =0.10 ± 0.02 MPa) and collagen (60 mg/mL, E0=0.57 ± 0.05 MPa) threads as well as mixed collagen:fibrin threads (3:2 in mass, E0 = 0.33 ± 0.05 MPa) and investigate the difference of affinity between primary murine myoblasts and tenoblasts. We demonstrate a similar behavior of cells on mixed and fibrin threads with high adherence of tenoblasts and myoblasts, in comparison to collagen threads that promote high adherence and proliferation of tenoblasts but not of myoblasts. Besides, we show that myoblasts on threads differentiate but do not fuse, on the contrary to 2D control substrates, raising the question of the effect of substrate curvature on the ability of myoblasts to fuse in vitro.

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“…“Ideal” IPNs should be co‐continuous networks of, for example, fibrin and another component; their composition should be roughly homogeneous at any level of scale, that is, taking molecule A and molecule B at a given composition, the same A/B ratio should be found at a macroscopic, microscopic or nanoscopic scale (Figure C, left). In real cases, IPNs may have a degree of phase separation (Figure C, middle), and this may extend to the point of one component being segregated in isolated domains (Figure C, right) . Fibrin‐based IPNs typically show higher moduli and an improved behavior with cells (above all less or slower contraction), and among the second components one should mention hyaluronic acid, which was cross‐linked via disulfide formation (thiol + 2‐pyridyl‐disulide) during fibrin formation; alginate, which gels thanks to the high calcium concentration of fibrinogen solutions; chitosan, which was cross‐linked by reacting in situ with a bis(formyl)PEG; PEG and poly(vinyl alcohol) (PVA), which are cured via photopolymerization of respectively terminal or side‐chain methacrylates. 3D‐printed structures .…”

Section: Fibrin As An Artificial Extracellular Matrixmentioning

confidence: 99%

Fibrin Matrices as (Injectable) Biomaterials: Formation, Clinical Use, and Molecular Engineering

Roberts

Bukhary

Leon‐Valdivieso

et al. 2019

Macromolecular Bioscience

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This review focuses on fibrin, starting from biological mechanisms (its production from fibrinogen and its enzymatic degradation), through its use as a medical device and as a biomaterial, and finally discussing the techniques used to add biological functions and/or improve its mechanical performance through its molecular engineering. Fibrin is a material of biological (human, and even patient's own) origin, injectable, adhesive, and remodellable by cells; further, it is nature's most common choice for an in situ forming, provisional matrix. Its widespread use in the clinic and in research is therefore completely unsurprising. There are, however, areas where its biomedical performance can be improved, namely achieving a better control over mechanical properties (and possibly higher modulus), slowing down degradation or incorporating cell-instructive functions (e.g., controlled delivery of growth factors).

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Mechanics of a two-fiber model with one nested fiber network, as applied to the collagen-fibrin system

Cited by 10 publications

References 48 publications

Type I Collagen-Fibrin Mixed Hydrogels: Preparation, Properties and Biomedical Applications

Type I Collagen-Fibrin Mixed Hydrogels: Preparation, Properties and Biomedical Applications

Differential myoblast and tenoblast affinity to collagen, fibrin and mixed threads in the prospect of muscle-tendon junction modelisation

Fibrin Matrices as (Injectable) Biomaterials: Formation, Clinical Use, and Molecular Engineering

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