Abstract:The affinity of metal ions for DNA is logical considering that the structure of DNA includes a phosphate backbone with a net-negative charge, a deoxyribose sugar with O atoms, and purine and pyrimidine bases that contain O and N atoms. DNA-metal ion interactions encompass a large area of research that ranges from the most fundamental characterization of DNA-metal ion binding to the role of DNA-bound metal ions in disease and human health. Alternative DNA base pairing mediated by metal binding is also being investigated and manipulated for applications in logic gates, molecular machines, and nanotechnology. This review highlights recent work aimed at understanding interactions of redox-active metal ions with DNA that provides a better understanding of the mechanisms by which various types of oxidative DNA damage (strand breakage and base modifications) occur. Antioxidants that mitigate oxidative DNA damage by coordinating metal ions that produce reactive oxygen species are addressed, as well as recent work on the effect of DNAmetal ion interactions and the efficacy of quinolone-based antibacterial drugs. Recent advances in metal-mediated base pairing that triggers conformational changes in DNA structure for use as selective metal ion sensors and novel nanotechnology applications are also included.
A novel reversed-phase (RP-) HPLC gradient profile applicable to multidimensional separations of complex protein mixtures is reported. This gradient profile elutes small numbers of proteins from the RP-HPLC column in discrete intervals while minimizing the amount of band broadening between elution intervals and maintaining constant flow through the HPLC column. Eluting the proteins in discrete intervals eases the instrumental requirements necessary for performing multidimensional separations and can be used to aid in the collection of well-defined fractions. The saw-tooth gradient was applied to the successful isolation of albumin from less abundant proteins in whole human serum and provides adequate separation of proteins in a low-molecular weight (LMW) fraction of human serum with resolution comparable to that achieved using a typical linear gradient profile.
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