Fibrin Fibers Have Extraordinary Extensibility and Elasticity

Liu, Wenhua; Jawerth, Louise; Sparks, Eric A.; Falvo, Michael R.; Hantgan, RR; Superfine, R.; Lord, Susan T.; Guthold, Martin

doi:10.1126/science.1127317

Cited by 246 publications

(235 citation statements)

References 6 publications

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“…We report an elastic modulus of 0.470 MPa (SD=0.107) for L-PRF membranes and stretch twice its initial length before failure (strain of 215%). These data match with published literature 22,23 who reported low stiffness (1-10 MPa) and high strain (up to 150%) before breaking. The difference in the values can be due to the use of fibrin network compared to the use of AFM analysis of single fibrin fiber in the above mentioned studies.…”

Section: Discussionsupporting

confidence: 82%

Characterization of Leukocyte-platelet Rich Fibrin, A Novel Biomaterial

Madurantakam

Yoganarasimha

Hasan

2015

JoVE

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Autologous platelet concentrates represent promising innovative tools in the field of regenerative medicine and have been extensively used in oral surgery. Unlike platelet rich plasma (PRP) that is a gel or a suspension, Leukocyte-Platelet Rich Fibrin (L-PRF) is a solid 3D fibrin membrane generated chair-side from whole blood containing no anti-coagulant. The membrane has a dense three dimensional fibrin matrix with enriched platelets and abundant growth factors. L-PRF is a popular adjunct in surgeries because of its superior handling characteristics as well as its suturability to the wound bed. The goal of the study is to demonstrate generation as well as provide detailed characterization of relevant properties of L-PRF that underlie its clinical success. Video LinkThe video component of this article can be found at

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Section: Discussionsupporting

confidence: 82%

Characterization of Leukocyte-platelet Rich Fibrin, A Novel Biomaterial

Madurantakam

Yoganarasimha

Hasan

2015

JoVE

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“…The large extensibility range of single fibrils of Fn and of other ECM proteins is thought to involve the unraveling of their secondary structure. 33,38,62,64,65 While the stress-strain relationship has not yet been established for Fn fibers, fibrin fibers (which have a comparable extensibility to those of Fn) show a stiffness increase at the presumed onset of module unfolding. 66,67 Our data may also offer a molecular level explanation for other experiments that have shown increases in ECM stiffness over time.…”

Section: Discussionmentioning

confidence: 99%

Fibronectin in aging extracellular matrix fibrils is progressively unfolded by cells and elicits an enhanced rigidity response

et al. 2008

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While the mechanical properties of a substrate or engineered scaffold can govern numerous aspects of cell behavior, cells quickly start to assemble their own matrix and will ultimately respond to their self-made extracellular matrix (ECM) microenvironments. Using fluorescence resonance energy transfer (FRET), we detected major changes in the conformation of a constituent ECM protein, fibronectin (Fn), as cells fabricated a thick three-dimensional (3D) matrix over the course of three days. These data provide the first evidence that matrix maturation occurs and that aging is associated with increased stretching of fibronectin fibrils, which leads to at least partial unfolding of the secondary structure of individual protein modules. A comparison of the conformations of Fn in these 3D matrices with those constructed by cells on rigid and flexible polyacrylamide surfaces suggests that cells in maturing matrices experience a microenviroment of gradually increasing rigidity. In addition, further matrix stiffening is caused by active Fn fiber alignment parallel to the contractile axis of the elongated fibroblasts, a cell-driven effect previously described for other fibrillar matrices. The fibroblasts, therefore, not only cause matrix unfolding, but reciprocally respond to the altered Fn matrix properties by up-regulating their own rigidity response. Consequently, our data demonstrate for the first time that a matured and aged matrix has distinctly different physical and biochemical properties compared to a newly assembled matrix. This might allow cells to specifically recognise the age of a matrix.

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“…Fibrin can then self-associate to form elongated, sometimes twisted, often highly branched fibers and fiber networks that, together with platelets and blood cells, form clots in response to vascular injury (1,(12)(13)(14)(15). Fibrin fibers are elastic and adhesive and show very high extensibility (16,17). Recent studies suggest that these properties derive, at least in part, from the properties of the fibrin molecule itself (18)(19)(20)(21).…”

mentioning

confidence: 99%

“…We investigate the physical properties of fibers suspended across the 25-m channels by using a combined fluorescence-atomic force microscope (AFM) system to monitor larger scale position and local fiber strain during pulls with the AFM tip (16,17). The regular channels result in fibrin polymers being suspended in situ 10 m above and parallel to the cover-glass surface.…”

mentioning

confidence: 99%

Ultrathin self-assembled fibrin sheets

Falvo

Millard²,

Eastwood

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Fibrin polymerizes into the fibrous network that is the major structural component of blood clots and thrombi. We demonstrate that fibrin from three different species can also spontaneously polymerize into extensive, molecularly thin, 2D sheets. Sheet assembly occurs in physiologic buffers on both hydrophobic and hydrophilic surfaces, but is routinely observed only when polymerized using very low concentrations of fibrinogen and thrombin. Sheets may have been missed in previous studies because they may be very short-lived at higher concentrations of fibrinogen and thrombin, and their thinness makes them very difficult to detect. We were able to distinguish fluorescently labeled fibrin sheets by polymerizing fibrin onto micropatterned structured surfaces that suspended polymers 10 m above and parallel to the cover-glass surface. We used a combined fluorescence/atomic force microscope system to determine that sheets were Ϸ5 nm thick, flat, elastic and mechanically continuous. Video microscopy of assembling sheets showed that they could polymerize across 25-m channels at hundreds of m 2 /sec (Ϸ10 13 subunits/s⅐M), an apparent rate constant many times greater than those of other protein polymers. Structural transitions from sheets to fibers were observed by fluorescence, transmission, and scanning electron microscopy. Sheets appeared to fold and roll up into larger fibers, and also to develop oval holes to form fiber networks that were ''preattached'' to the substrate and other fibers. We propose a model of fiber formation from sheets and compare it with current models of end-wise polymerization from protofibrils. Sheets could be an unanticipated factor in clot formation and adhesion in vivo, and are a unique material in their own right.clot ͉ fiber ͉ monomolecular sheet ͉ network ͉ thrombus B ecause of the central role of fibrin in the clotting of blood during wound healing and in the formation of pathogenic vascular thrombi, the polymerization of fibrin has been actively studied since the mid-19th century (1). The parent protein, fibrinogen, is an elongated, sausage-shaped dimeric molecule with symmetry around a central globular domain (2-6). Cleavage and removal of the small peptides-fibrinopeptide A and later B-from fibrinogen by the enzyme thrombin expose specific binding sites (''knobs'') on fibrin that allow binding to corresponding regions (''holes'') on neighboring fibrin molecules (7-11). Fibrin can then self-associate to form elongated, sometimes twisted, often highly branched fibers and fiber networks that, together with platelets and blood cells, form clots in response to vascular injury (1,(12)(13)(14)(15). Fibrin fibers are elastic and adhesive and show very high extensibility (16,17). Recent studies suggest that these properties derive, at least in part, from the properties of the fibrin molecule itself (18-21). Exhaustive studies of fibrin polymerization in vitro have been carried out with purified components since the 1940s (e.g., 22, 23), but several details of fibrin assembly into fibers and fibe...

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Fibrin Fibers Have Extraordinary Extensibility and Elasticity

Cited by 246 publications

References 6 publications

Characterization of Leukocyte-platelet Rich Fibrin, A Novel Biomaterial

Characterization of Leukocyte-platelet Rich Fibrin, A Novel Biomaterial

Fibronectin in aging extracellular matrix fibrils is progressively unfolded by cells and elicits an enhanced rigidity response

Ultrathin self-assembled fibrin sheets

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