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Researchers from Jacobs University Discuss Findings in Biochemistry (Dynamically Analyte-Responsive Macrocyclic Host-Fluorophore Systems)

August 20, 2014

By a News Reporter-Staff News Editor at Biotech Week -- Data detailed on Biochemistry have been presented. According to news reporting originating from Bremen, Germany, by NewsRx correspondents, research stated, "CONSPECTUS: Host-guest chemistry commenced to a large degree with the work of Pedersen, who in 1967 first reported the synthesis of crown ethers. The past 45 years have witnessed a substantial progress in the field, from the design of highly selective host molecules as receptors to their application in drug delivery and, particularly, analyte sensing."

Our news editors obtained a quote from the research from Jacobs University, "Much effort has been expended on designing receptors and signaling mechanism for detecting compounds of biological and environmental relevance. Traditionally, the design of a chemosensor comprises one component for molecular recognition, frequently macrocycles of the cyclodextrin, cucurbituril, cyclophane, or calixarene type. The second component, used for signaling, is typically an indicator dye which changes its photophysical properties, preferably its fluorescence, upon analyte binding. A variety of signal transduction mechanisms are available, of which displacement of the dye from the macrocyclic binding site is one of the simplest and most popular ones. This constitutes the working principle of indicator displacement assays. However, indicator displacement assays have been predominantly exploited in a static fashion, namely, to determine absolute analyte concentrations, or, by using combinations of several reporter pairs, to achieve a differential sensing and, thus, identification of specific food products or brands. In contrast, their use in biological systems, for example, with membranes, cells, or with enzymes has been comparably less explored, which led us to the design of the so-called tandem assays, that is, dynamically analyte-responsive host-dye systems, in which the change in analyte concentrations is induced by a biological reaction or process. This methodological variation has practical application potential, because the ability to monitor these biochemical pathways or to follow specific molecules in real time is of paramount interest for both biochemical laboratories and the pharmaceutical industry. We will begin by describing the underlying principles that govern the use of macrocycle-fluorescent dye complexes to monitor time-dependent changes in analyte concentrations. Suitable chemosensing ensembles are introduced, along with their fluorescence responses (switch-on or switch-off). This includes supramolecular tandem assays in their product- and substrate-selective variants, and in their domino and enzyme-coupled modifications, with assays for amino acid decarboxylases, diamine, and choline oxidase, proteases, methyl transferases, acetylcholineesterase (including an unpublished direct tandem assay), choline oxidase, and potato apyrase as examples. It also includes the very recently introduced tandem membrane assays in their published influx and unpublished efflux variants, with the outer membrane protein F as channel protein and protamine as bidirectionally translocated analyte."

According to the news editors, the research concluded: "As proof-of-principle for environmental monitoring applications, we describe sensing ensembles for volatile hydrocarbons."

For more information on this research see: Dynamically Analyte-Responsive Macrocyclic Host-Fluorophore Systems. Accounts of Chemical Research, 2014;47(7):2150-2159. Accounts of Chemical Research can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society -; Accounts of Chemical Research -

The news editors report that additional information may be obtained by contacting G. Ghale, Jacobs Univ Bremen, Sch Engn & Sci, D-28759 Bremen, Germany (see also Biochemistry).

Keywords for this news article include: Bremen, Europe, Germany, Oxidase, Biochemical, Biochemistry, Enzymes and Coenzymes

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Source: Biotech Week

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