Collapse mechanism maps for the hollow pyramidal core of a sandwich panel under transverse shear

The finite element method has been used to develop collapse mechanism maps for the shear response of sandwich panels with a stainless steel core comprising hollow struts. The core topology comprises either vertical tubes or inclined tubes in a pyramidal arrangement. The dependence of the elastic and plastic buckling modes upon core geometry is determined, and optimal geometric designs are obtained as a function of core density. For the hollow pyramidal core, strength depends primarily upon the relative density ρ̄ of the core with a weak dependence upon tube slenderness. At ρ̄ below about 3%, the tubes of the pyramidal core buckle plastically and the peak shear strength scales linearly with ρ̄. In contrast, at ρ̄ above 3%, the tubes do not buckle and a stable shear response is observed. The predictions of the current study are in excellent agreement with previous measurements on the shear strength of the hollow pyramidal core, and suggest that this core topology is attractive from the perspectives of both core strength and energy absorption. © 2011 Elsevier Ltd. All rights reserved.

An assessment of the blast resistance of sandwich beams

An assessment of the underwater blast resistance of sandwich beams with a prismatic Y-truss core is presented, utilizing three-dimensional finite element calculations. Results show a significant performance benefit for sandwich construction when compared to a monolithic plate of the same mass when the sandwich core combines high shear strength with low compressive strength.

Interfacial recognition of human prostate-specific antigen by immobilized monoclonal antibody: effects of solution conditions and surface chemistry.

The specific recognition between monoclonal antibody (anti-human prostate-specific antigen, anti-hPSA) and its antigen (human prostate-specific antigen, hPSA) has promising applications in prostate cancer diagnostics and other biosensor applications. However, because of steric constraints associated with interfacial packing and molecular orientations, the binding efficiency is often very low. In this study, spectroscopic ellipsometry and neutron reflection have been used to investigate how solution pH, salt concentration and surface chemistry affect antibody adsorption and subsequent antigen binding. The adsorbed amount of antibody was found to vary with pH and the maximum adsorption occurred between pH 5 and 6, close to the isoelectric point of the antibody. By contrast, the highest antigen binding efficiency occurred close to the neutral pH. Increasing the ionic strength reduced antibody adsorbed amount at the silica-water interface but had little effect on antigen binding. Further studies of antibody adsorption on hydrophobic C8 (octyltrimethoxysilane) surface and chemical attachment of antibody on (3-mercaptopropyl)trimethoxysilane/4-maleimidobutyric acid N-hydroxysuccinimide ester-modified surface have also been undertaken. It was found that on all surfaces studied, the antibody predominantly adopted the 'flat on' orientation, and antigen-binding capabilities were comparable. The results indicate that antibody immobilization via appropriate physical adsorption can replace elaborate interfacial molecular engineering involving complex covalent attachments.