Influencing biophysical properties of fibrin with buffer solutions

Potier, Esther; Noailly, Jérôme; Sprecher, Christoph M.; Ito, Keita

doi:10.1007/s10853-010-4221-1

Cited by 11 publications

(9 citation statements)

References 36 publications

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“…The solution was kept at 37°C for 10 min before further usage to allow complete cleavage of FXIII. To form stabilized fibrin hydrogel, FXIIIa with a final concentration of 8 U/ml was added to a gel with fibrinogen (7.5 mg/ml) ( 28 , 46 ).…”

Section: Methodsmentioning

confidence: 99%

Microscale spatial heterogeneity of protein structural transitions in fibrin matrices

2016

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Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support large strains associated with tissue movement around the wound. These combined properties are enabled by a fibrous matrix consisting of the protein fibrin. Fibrin hydrogels can support large macroscopic strains owing to the unfolding transition of a-helical fibril structures to b sheets at the molecular level, among other reasons. Imaging protein secondary structure on the submicrometer length scale, we reveal that another length scale is relevant for fibrin function. We observe that the protein polymorphism in the gel becomes spatially heterogeneous on a micrometer length scale with increasing tensile strain, directly showing load-bearing inhomogeneity and nonaffinity. Supramolecular structural features in the hydrogel observed under strain indicate that a uniform fibrin hydrogel develops a composite-like microstructure in tension, even in the absence of cellular inclusions.

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Section: Methodsmentioning

confidence: 99%

Microscale spatial heterogeneity of protein structural transitions in fibrin matrices

2016

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“…If fibrin concentrations remain constant and thrombin concentrations are varied, low concentrations of thrombin lead to the formation of turbid fibrin gels consisting of thick fibers, few branch points and large pores, while higher concentrations of thrombin lead to the formation of less turbid gels consisting of tightly packed thin fibers. Increasing calcium concentration has been shown to result in the formation of more turbid gels with increased fiber size but lower rigidity [52, 135–137]. Increasing salt concentration, while utilizing low calcium concentrations (2mM) results in less turbid gels [135].…”

Section: Modulation Of Fibrin Propertiesmentioning

confidence: 99%

“…Increasing calcium concentration has been shown to result in the formation of more turbid gels with increased fiber size but lower rigidity [52, 135–137]. Increasing salt concentration, while utilizing low calcium concentrations (2mM) results in less turbid gels [135]. Furthermore, gel stiffness correlates with fibrinogen and thrombin concentration, with fibrinogen concentration affecting stiffness to a greater degree than thrombin concentration.…”

Section: Modulation Of Fibrin Propertiesmentioning

confidence: 99%

Fibrin-based biomaterials: Modulation of macroscopic properties through rational design at the molecular level

2014

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Fibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury. Because of these properties and the ease of polymerization of the material, fibrin has been widely utilized as a biomaterial for over a century. Modifying the macroscopic properties of fibrin, such as elasticity and porosity, has been somewhat elusive until recently, yet with a molecular-level rational design approach can now be somewhat easily modified through alterations of molecular interactions key to the protein’s polymerization process. This review outlines the biochemistry of fibrin and discusses methods for modification of molecular interactions and their application to fibrin based biomaterials.

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“…Now observable are regions of densely collapsed, interconnected fibers and large, three-dimensional voids not seen in the buffered sample (Figure c). Although the unique damage in the salt-only case is clearly significant and ascribable to rampant radical reactivity, it should be noted that the reaggregation of disturbed fragments is also subject to electrostatic effects from environmental conditions and buffer composition …”

Section: Resultsmentioning

confidence: 99%

Non-Enzymatic Remodeling of Fibrin Biopolymers via Photothermally Triggered Radical-Generating Nanoparticles

Walker

Zaleski

2014

Chem. Mater.

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Thrombosis is a hallmark of several chronic diseases leading to potentially fatal heart attacks and strokes. Frontline interventions include intravenous delivery of potent, enzymatic fibrinolytics that possess a high risk for inducing systemic bleeding. As a conceptual countermeasure, we have developed a water-soluble PEGylated gold nanoparticle appended with the enediyne diamine (Z)-octa-4-en-2,6-diyne-1,8-diamine that is capable of photothermally generating 1,4-diradical species under visible excitation (λ = 514 nm, 100 mW, 2−6 h). In the absence of biopolymer substrate, photothermal excitation of these particles leads to self-quenching polymer coating formation in water. When these radical-generating nanoparticles are intrinsically applied toward the blood clot structural protein assembly fibrin, as well as its nonpolymerized precursor protein fibrinogen, scanning electron microscopy images reveal significantly modified fibrin clot morphology, as evidenced by larger void spaces and collapsed fiber regions. Quantitatively, laser confocal microscopy images of Alexa Fluor 488-labeled fibrin clots extrinsically treated with nanoparticles at the clot/solution interface show that photothermal radical formation by these particles leads to marked increase in the number of larger pore sizes (>2.0 μm) within the fibrin matrix, which derive from a corresponding decrease in the histogram of smaller pore sizes (1.5−2.0 μm). These larger pore sizes ultimately result in total perfusion of solution through the entire clot volume. The chemical manifestation of this is that radical-induced modifications occur mainly at the protein level but lead to morphological changes at the micron scale. Overall, this technology could have significant impact for disease states such as deep vein thrombosis via a localized, catheter-delivered approach.

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Influencing biophysical properties of fibrin with buffer solutions

Cited by 11 publications

References 36 publications

Microscale spatial heterogeneity of protein structural transitions in fibrin matrices

Microscale spatial heterogeneity of protein structural transitions in fibrin matrices

Fibrin-based biomaterials: Modulation of macroscopic properties through rational design at the molecular level

Non-Enzymatic Remodeling of Fibrin Biopolymers via Photothermally Triggered Radical-Generating Nanoparticles

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