In Situ Synthesis Of Nanocrystalline Intermetallic Layer During Surface Plastic Deformation Of Zirconium

By means of a surface plastic deformation method a nanocrystalline (NC) intermetallic compound was in situ synthesized on the surface layer of bulk zirconium (Zr). Hardened steel shots (composition: 1.0C, 1.5Cr, base Fe in wt.%) were used to conduct repetitive and multidirectional peening on the surface layer of Zr. The microstructure evolution of the surface layer was investigated by X-ray diffraction and scanning and transmission electron microscopy observations. The NC intermetallic layer of about 25 gm thick was observed and confirmed by concentration profiles of Zr, Fe and Cr, and was found to consist of the Fe100-xCrx compound with an average grain size of 22 nm. The NC surface layer exhibited an extremely high average hardness of 10.2 GPa. The Zr base immediately next to the compound/Zr interface has a grain size of similar to 250 nm, and a hardness of similar to 3.4 GPa. The Fe100-xCrx layer was found to securely adhere to the Zr base. (c) 2007 Elsevier B.V All rights reserved.

Measuring Binding Kinetics Of Surface-Bound Molecules Using The Surface Plasmon Resonance Technique

Surface plasmon resonance (SPR) technology and the Biacore biosensor have been widely used to measure the kinetics of biomolecular interactions in the fluid phase. In the past decade, the assay was further extended to measure reaction kinetics when two counterpart molecules are anchored on apposed surfaces. However, the cell binding kinetics has not been well quantified. Here we report development of a cellular kinetic model, combined with experimental procedures for cell binding kinetic measurements, to predict kinetic rates per cell. Human red blood cells coated with bovine serum albumin and anti-BSA monoclonal antibodies (mAbs) immobilized on the chip were used to conduct the measurements. Sensor-grams for BSA-coated RBC binding onto and debinding from the anti-BSA mAb-immobilized chip were obtained using a commercial Biacore 3000 biosensor, and analyzed with the cellular kinetic model developed. Not only did the model fit the data well, but it also predicted cellular on and off-rates as well as binding affinities from curve fitting. The dependence of flow duration, flow rate, and site density of BSA on binding kinetics was tested systematically, which further validated the feasibility and reliability of the new approach. Crown copyright (c) 2008 Published by Elsevier Inc. All rights reserved.

Surface-Bound Selectin-Ligand Binding Is Regulated By Carrier Diffusion

Two-dimensional (2D) kinetics of receptor-ligand interactions governs cell adhesion in many biological processes. While the dissociation kinetics of receptor-ligand bond is extensively investigated, the association kinetics has much less been quantified. Recently receptor-ligand interactions between two surfaces were investigated using a thermal fluctuation assay upon biomembrane force probe technique (Chen et al. in Biophys J 94:694-701, 2008). The regulating factors on association kinetics, however, are not well characterized. Here we developed an alternative thermal fluctuation assay using optical trap technique, which enables to visualize consecutive binding-unbinding transition and to quantify the impact of microbead diffusion on receptor-ligand binding. Three selectin constructs (sLs, sPs, and PLE) and their ligand P-selectin glycoprotein ligand 1 were used to conduct the measurements. It was indicated that bond formation was reduced by enhancing the diffusivity of selectin-coupled carrier, suggesting that carrier diffusion is crucial to determine receptor-ligand binding. It was also found that 2D forward rate predicted upon first-order kinetics was in the order of sPs > sLs > PLE and bond formation was history-dependent. These results further the understandings in regulating association kinetics of surface-bound receptor-ligand interactions.