Integrated barcode chips for rapid, multiplexed analysis of proteins in microliter quantities of blood.

As the tissue that contains the largest representation of the human proteome, blood is the most important fluid for clinical diagnostics. However, although changes of plasma protein profiles reflect physiological or pathological conditions associated with many human diseases, only a handful of plasma proteins are routinely used in clinical tests. Reasons for this include the intrinsic complexity of the plasma proteome, the heterogeneity of human diseases and the rapid degradation of proteins in sampled blood.

On the mechanism of lead chalcogenide nanocrystal formation.

On the basis of evidence from 31P NMR spectroscopy, and using PbSe as a model, we propose two simultaneous mechanisms through which "monomers" are formed in preparations of lead chalcogenide nanocrystals (NCs). In one mechanism, selenium is delivered as a Se2- species, whereas in the other, Se0 reacts with metal already reduced by the organophosphine. This latter mechanism helps explain the sensitivity of NC preparations to the purity of organophosphines and allows the rational modification of batch NC reactions to increase yield.

Influence of microstructure on the electrochemical performance of tin-doped indium oxide film electrodes.

The effect of the microstructure of tin-doped indium oxide (ITO) films on their electrochemical performance was studied using three redox probes, tris(2,2'-bipyridyl ruthenium(II) chloride (Ru(bpy)3(2+/3+)), ferrocyanide (Fe(CN)6(4-/3-)), and ferrocenemethanol (FcCH2H(0/+)). ITO films were deposited using dc magnetron sputtering under a variety of conditions that resulted in films having different degrees of crystallinity, crystallographic texture, sheet resistance, surface roughness, and percent tin. It was found that the electron transfer for all three redox probes used in this study was more efficient at polycrystalline films than at amorphous ITO films.