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Proposed Mode (proposed + mode)

Distribution by Scientific Domains

Chemistry	50%

Selected Abstracts

Tellurium-Based Polymeric Surfactants as a Novel Seleno-Enzyme Model with High Activity

MACROMOLECULAR RAPID COMMUNICATIONS, Issue 24 2006
Xin Huang
Abstract Summary: A tellurium-based polymeric sufactant as a seleno-enzyme model has been constructed by employing 11-acryloyloxyundecyltriethylammonium bromide (AUTEAB, 4) and a tellurium-containing compound (1). It demonstrates strong substrate binding ability for thiols and high glutathione peroxidase (GPx) activity about 6 orders of magnitude more efficient than the well-known GPx mimic PhSeSePh in an ArSH assay system. More importantly, a series of tellurium-based polymeric micelle catalysts with the catalytic tellurium center located at various positions in the micelle have been constructed, and the dramatic difference in activity indicates that the exact match of the catalytic center and binding site plays a key role in enzyme catalytic efficiency. Schematic representation of the proposed mode of the telluro-micelle catalysts. [source]

Quest for the Molecular Mechanism of Chromium Action and Its Relationship to Diabetes

NUTRITION REVIEWS, Issue 3 2000
John B. Vincent Ph.D.
Despite forty years of research on the potential role of chromium in carbohydrate and lipid metabolism, significant progress has only recently been made regarding the mode of action of chromium at a molecular level. The oligopeptide low-molecular-weight chromium-binding substance (LMWCr) may function as part of a novel insulin-signaling autoamplification mechanism. The proposed mechanism of action also sheds some light on the potential of chromium-containing compounds as nutritional supplements or in the treatment of adult-onset diabetes and other conditions. The potential relationship between the results of recent studies on diabetic patients and the proposed mode of action of LMWCr are discussed. [source]

Equalizer technology , Equal rights for disparate beads

PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 11 2010
Eva-Maria Keidel
Abstract One major limitation in proteomics is the detection and analysis of low-abundant proteins, i.e. in plasma. Several years ago, a technique to selectively enrich the relative concentration of low-abundant proteins was introduced by Boschetti and co-workers. It is based on a specific and saturable interaction of proteins to a high diversity of binding sites, realized by a hexapeptide library coupled to beads. This technology was commercialized as Equalizer beads or ProteoMiner. However, during application of ProteoMiner beads to plasma samples unexpected results questioned the proposed mode of action. Therefore, ProteoMiner beads were compared with chromatographic beads exhibiting completely different surface chemistry. Sepabeads FP-OD400 octadecyl, FP-DA400 diethylamine, FP-BU400 butyl, FP-HG400 hydroxyl and EXE056 epoxy were used. The results show that ProteoMiner or the different Sepabeads behave surprisingly similarly in the separation of complex protein mixtures. ProteoMiner beads interact with protein mixtures according to a general hydrophobic binding mechanism, where diversity in surface ligands plays only a negligible role. [source]

KP1019, A New Redox-Active Anticancer Agent , Preclinical Development and Results of a Clinical Phase I Study in Tumor Patients

CHEMISTRY & BIODIVERSITY, Issue 10 2008
Christian
Abstract The promising drug candidate indazolium trans -[tetrachlorobis(1H -indazole)ruthenate(III)] (KP1019) is the second Ru-based anticancer agent to enter clinical trials. In this review, which is an update of a paper from 2006 (Hartinger et,al., J. Inorg. Biochem.2006, 100, 891,904), the experimental evidence for the proposed mode of action of this coordination compound is discussed, including transport into the cell via the transferrin cycle and activation by reduction. The results of the early clinical development of KP1019 are summarized in which five out of six evaluated patients experienced disease stabilization with no severe side effects. [source]