1. Optical Biosensor Detects Biological Toxins and Infectious Agents
Synthesis, Structural Characterization and Property Optimization of Novel Antimonides and Bismuthides
Svilen Bobev Department of Chemistry and Biochemistry, University of Delaware Newark, DE 19716
A new ternary compound Ba3Cd2Sb4 has been synthesized and structurally characterized by single-crystal X-ray diffraction. The compound crystallizes in monoclinic crystal system, in the space group C2/m, and its structure can be viewed as two-dimensional [Cd2Sb4] layers made up of CdSb4 tetrahedra, separated by Ba cations. The tetrahedra are edge-shared and linked through Sb2 dimers. Concerning the structure, a number of analogies could be drawn with other known structure types, featuring similar building blocks, such as the Ca5Al2Sb6 structure, the Ca2CdSb2 and Yb2CdSb2 structures, and of course, the TiNiSi structure. Although reactions intended to make a series of isostructutural compounds failed, four mixed Ba3–xAxCd2Sb4 phases, where A = Ca, Sr, Eu, Yb, were also synthesized. It was observed, that in all four compounds, only the inter-layer barium atoms can be replaced. TB-LMTO calculations showed that the inter-layer barium site has higher electron density and interactions of inter-layer atoms with surrounding antimony atoms show stronger covalent character. The results of calculations also show that even though interlayer Ba atoms are more likely to be replaced, barium atoms themselves are favored more in that position..
Optical Biosensor Detects Biological Toxins and Infectious Agents
Toxins (poisons produced by living organisms) and disease-causing organisms such as viruses work by binding to specific receptors on the surface of an affected cell. Binding causes the receptors to aggregate, allowing the toxin or invading virus to enter the cell.
Our Optical Biosensor uses optically tagged natural receptors embedded in a synthetic cell membrane to mimic a natural chain of events. When a target protein binds, the receptors in the cell membrane are pulled into a cluster by the toxin’s binding sites (shown for cholera toxin in red). The close proximity of the receptors, which are normally further apart, triggers an energy transfer leading to a fluorescent response.