Rheology of fibrin clots

Nelb, Gary W.; Gerth, Christian; Ferry, John D.; Lóránd, L.

doi:10.1016/0301-4622(76)80050-6

Cited by 82 publications

(15 citation statements)

References 13 publications

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“…Both fibrin and collagen are known to display strain-hardening in response to a tensile load [22; 28; 31; 32]. In addition, fibrin was shown to stiffen under compression at high strains [40].…”

Section: Discussionmentioning

confidence: 99%

“…In collagen, strain-stiffening may contribute to cell and tissue integrity under mechanical deformations [30]. Both materials also indicate viscoelastic properties under shear or compression, as they are able to recover deformations as well as to relax internal stresses via dissipation [31; 40; 52]. Additionally, when exposed to repeating large-shear-strain loading, these biopolymers are characterized by a shift of the nonlinear stress response to higher strains due to lengthening of individual fibers [53] associated with interplay between bending and buckling of fibers.…”

Section: Discussionmentioning

confidence: 99%

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Compression-induced structural and mechanical changes of fibrin-collagen composites

et al. 2017

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Fibrin and collagen as well as their combinations play an important biological role in tissue regeneration and are widely employed in surgery as fleeces or sealants and in bioengineering as tissue scaffolds. Earlier studies demonstrated that fibrin-collagen composite networks displayed improved tensile mechanical properties compared to the isolated protein matrices. Unlike previous studies, here unconfined compression was applied to a fibrin-collagen filamentous polymer composite matrix to study its structural and mechanical responses to compressive deformation. Combining collagen with fibrin resulted in formation of a composite hydrogel exhibiting synergistic mechanical properties compared to the isolated fibrin and collagen matrices. Specifically, the composite matrix revealed a one order of magnitude increase in the shear storage modulus at compressive strains > 0.8 in response to compression compared to the mechanical features of individual components. These material enhancements were attributed to the observed structural alterations, such as network density changes, an increase in connectivity along with criss-crossing, and bundling of fibers. In addition, the compressed composite collagen/fibrin networks revealed a non-linear transformation of their viscoelastic properties with softening and stiffening regimes. These transitions were shown to depend on protein concentrations. Namely, a decrease in protein content drastically affected the mechanical response of the networks to compression by shifting the onset of stiffening to higher degrees of compression. Since both natural and artificially composed extracellular matrices experience compression in various (patho)physiological conditions, our results provide new insights into the structural biomechanics of the polymeric composite matrix that can help to create fibrin-collagen sealants, sponges, and tissue scaffolds with tunable and predictable mechanical properties.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Compression-induced structural and mechanical changes of fibrin-collagen composites

et al. 2017

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“…This material is easily formed and handled, and combines the outstanding mechanical properties of the ELRs with the well-known cell-affinity of the fibrin gels [39][40][41][42] , improving the elastic properties with respect to pure fibrin gels. A poroelastic mechanism dominates the viscoelastic behaviour in the range of the analysed frequencies.…”

Section: Discussionmentioning

confidence: 99%

Hybrid elastin-like recombinamer-fibrin gels: physical characterization and in vitro evaluation for cardiovascular tissue engineering applications

et al. 2016

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In the field of tissue engineering, the properties of the scaffolds are of crucial importance for the success of the application. Hybrid materials combine properties of the different components that constitute them. In this study hybrid gels of elastin-like recombinamer (ELR) and fibrin were prepared with a range on polymer concentrations and ELR-to-fibrin ratios. The correlation between SEM micrographs, porosity, swelling ratio and rheological properties was discussed and a poroelastic mechanism was suggested to explain the mechanical behavior of the hybrid gels. Applicability as scaffold material for cardiovascular tissue engineering was shown by the realization of cell-laden matrixes which supported the synthesis of collagens as revealed by immunohistochemical analysis. As a proof of concept, a tissue-engineered heart valve was fabricated by injection moulding and cultivated in a bioreactor for 3 weeks under dynamic conditions. Tissue analysis revealed production of collagen I and III, fundamental proteins for cardiovascular constructs.

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“…A similar difference is seen in comparing the moduli of fine and coarse fibrin clots, in which the fibrin concentration is much smaller. 12 Plots of stress relaxation over time periods up to about…”

Section: Resultsmentioning

confidence: 99%

Preparation of two‐dimensionally oriented elastic films from fibrin clots and other protein gels

Müller

Ferry

1984

Biotech & Bioengineering

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Fibrin film, an elastic sheet prepared from a fibrin clot, was first described in 1944.' The precursor is a fibrin clot of the type designated as "coarse," whose fiber structure consists of thick bundles of protofibrils formed in the natural blood coagulation process, containing 5 to 10 mg/mL of fibrin protein, the remainder being buffer solution. This is gently compacted in one dimension with syneresis of buffer solution to reduce the thickness by a factor of the order of 20 while the area remains essentially ~n c h a n g e d .~,~ The natural structure is preserved except that its fibrous elements lie primarily in the plane of the film, though oriented at random within that plane. This fibrin film can be stretched 100% with subsequent elastic recovery after release of tension. It has been used in surgical applications4 and has been the subject of several recent investigations to elucidate fibrin s t r u c t~r e .~-~ The width of the fibers comprising the fibrin clot structure can be decreased by increasing the pH and ionic strength at which clotting by thrombin takes place, culminating in the "fine" clot in which the fibrous elements consist of single protofibrilss or segments of two or three twisted t~g e t h e r .~ Such a clot does not synerize and cannot be compacted under pressure. However, it has now been found possible to remove the buffer by osmosis to compact a fine clot in one dimension and prepare a fine fibrin film that has similar elastic properties. Moreover, the same method can be applied to other fragile protein gels such as gelatin and denatured serum albumin. The resulting protein films may have various practical applications. MATERIALS AND METHODSBovine fibrinogen (Miles Laboratories, 95% clottable) was dissolved in and dialyzed against a large volume of sodium chloride-imidazole buffer, pH 8.5, ionic strength 0.41. A solution containing 10 g/L of fibrinogen with 2 units/mL of Trasylol (proteolytic inhibitor, from FBA pharmaceuticals) and 0.003M calcium chloride (to introduce y-y covalent bonds by ligation-sufficient fibrin stabilizing factor, Factor XIII, being present as a desired Biotechnology and Bioengineering, Vol. XXVI, Pp. 191-193 (1984) impurity) was mixed with sufficient thrombin (bovine, from Parke, Davis, and Company) to give a specified clotting time, usually about 10 min, and poured into a 2 X 5 in. polyethylene tray. The resulting transparent clot was allowed to stand at room temperature, covered by a lid, for at least 16 h to allow the structure to become fully developed. 5,9 A sample of pigskin gelatin was generously provided by Rousselot S . A. (Paris; France); it had been used in other investigations in this laboratory.lO.il Its isoelectric point was 7.0, the pH of an aqueous solution was 5.1, and the number-average molecular weight was 3.5 X lo4. It was dissolved in water at 50°C at a concentration of 6% by weight. The solution was kept in the covered polyethylene tray for 15 h at 7OoC to erase any aggregation history, then cooled to room temperature and held for 5 h.Bov...

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Rheology of fibrin clots

Cited by 82 publications

References 13 publications

Compression-induced structural and mechanical changes of fibrin-collagen composites

Compression-induced structural and mechanical changes of fibrin-collagen composites

Hybrid elastin-like recombinamer-fibrin gels: physical characterization and in vitro evaluation for cardiovascular tissue engineering applications

Preparation of two‐dimensionally oriented elastic films from fibrin clots and other protein gels

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