Shear Modulation Force Microscopy (SMFM) together with the Atomic Force Microscopy (AFM) based three-point bending technique were used to measure the mechanical properties of electrospun polymers and polymer nanocomposite fibers. Both techniques showed that the moduli of the fibers increased significantly with decreasing fiber diameter. We attributed this enhancement to the orientation of polymer chains which occurs during the electrospinning process. We then predicted, and confirmed experimentally, that the phenomenon scales with Rg rather than with the absolute fiber diameter and can propagate radially for large distances (∼20Rg) into the fiber interior. The inclusion of nanotubes into the fibers further enhanced the orientation by introducing additional surfaces. The additional increase in modulus (more than an order of magnitude) could then be explained by the same model and scaled on a universal curve .
Wound healing is a complex process initiated by the formation of fibrin fibers and endothelialization. Normally, this process is triggered in a wound by thrombin cleavage of fibrinopeptides on fibrinogen molecules, which allows them to self spontaneously-assemble into large fibers that provide the support structure of the clot and promote healing. We have found that the fibrous structures can also form without thrombin on most polymer or metal surfaces, including those commonly used for stents. We show that the relatively hydrophobic E and D regions of the fibrinogen molecule are adsorbed on these surfaces, exposing the αC domains, which in turn results in the formation of large fiber structures that promote endothelial cell adhesion. We show that the entire process can be suppressed when stents or other substrates are coated with polymers that are functionalized to bind the αC domains, leading to the development of potentially nonthrombogenic implant materials.
By embedding "dilute" gold nanoparticles in single polystyrene thin films as "markers", we probe the local viscosity of the free surface at temperatures far above the glass transition temperature (T(g)). The technique used was x-ray photon correlation spectroscopy with resonance-enhanced x-ray scattering. The results clearly showed the surface viscosity is about 30% lower than the rest of the film. We found that this reduction is strongly associated with chain entanglements at the free surface rather than the reduction in T(g).
Summary. Background: Exposure of cryptic, functional sites on fibrinogen upon its adsorption to hydrophobic surfaces of biomaterials has been linked to an inflammatory response and fibrosis. Such adsorption also induces ordered fibrinogen aggregation which is poorly understood. Objective: To investigate hydrophobic surface-induced fibrinogen aggregation. Methods: Contact and lateral force scanning probe microscopy, yielding topography, image dimensions and fiber elastic modulus measurements were used along with transmission and scanning electron microscopy. Fibrinogen aggregation was induced under non-enzymatic conditions by adsorption on a trioctyl-surface monolayer (trioctylmethylamine) grafted onto silica clay plates. Results: A more than one molecule thick coating was generated by adsorption on the plate from 100 to 200 lg mL )1 fibrinogen solutions, and three-dimensional networks formed from 4 mg mL )1 fibrinogen incubated with uncoated or fibrinogen-coated plates. Fibrils appeared laterally assembled into branching and overlapping fibers whose heights from the surface ranged from approximately 3 to 740 nm. The elastic modulus of fibrinogen fibers was 1.55 MPa. No fibrils formed when fibrinogen lacking aC-domains was used as a coating or was incubated with intact fibrinogen-coated plates, or when the latter plates were sequentially incubated with antiAa529-539 mAb and intact fibrinogen. When an anti-Aa241-476 mAb was used instead, fine, long fibers formed. Similarly, sequential incubations of fibrinogen-coated plates with recombinant aC-domain (Aa392-610 fragment) or aC-connector (Aa221-372 fragment) and fibrinogen resulted in distinctly fine fiber networks. Conclusions: Adsorption-induced fibrinogen self-assembly is initiated by a more than one molecule-thick surface layer and eventuates in three-dimensional networks whose formation requires fibrinogen with intact aC-domains.
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