Mechanisms of projectile penetration in Dyneema® encapsulated aluminum structures

Polymer composites comprising ultra-high molecular weight polyethylene (UHWMPE) fibers in a compliant matrix are now widely used in ballistic applications with varying levels of success. This is primarily due to a poor understanding of the mechanics of penetration of these composites in ballistic protection systems. In this study, we report experimental observations of the penetration mechanisms in four model systems impacted by a 12.7 mm diameter spherical steel projectile. The four model targets designed to highlight different penetration mechanisms in Dyneema® UHWMPE composites were: (i) a bare aluminum plate; (ii) the same plate fully encased in a 5.9 mm thick casing of Dyneema®; (iii) the fully encased plate with a portion of the Dyneema® removed from the front face so that the projectile impacts directly the Al plate; and (iv) the fully encased plate with a portion of the Dyneema® removed from the rear face so that the projectile can exit the Al plate without again interacting with the Dyneema®. A combination of synchronized high speed photography with three cameras, together with post-test examination of the targets via X-ray tomography and optical microscopy was used to elucidate the deformation and perforation mechanisms. The measurements show that the ballistic resistance of these targets increases in the order: bare Al plate, rear face cutout target, fully encased target and front face cutout target. These findings are explained based on the following key findings: (a) the ballistic performance of Dyneema® plates supported on a foundation is inferior to Dyneema® plates supported along their edges; (b) the apparent ballistic resistance of Dyneema® plates increases if the plates are given an initial velocity prior to the impact by the projectile, thereby reducing the relative velocity between the Dyneema® plate and projectile; and (c) when the projectile is fragmented prior to impact, the spatially and temporally distributed loading enhances the ballistic resistance of the Dyneema®. The simple model targets designed here have elucidated mechanisms by which Dyneema® functions in multi-material structures. © 2014 Elsevier Ltd.

Effect of the interplay between protein and surface on the properties of adsorbed protein layers.

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials.

Effect of the interplay between protein and surface on the properties of adsorbed protein layers

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials. © 2014 The Authors.