197850-75-2Relevant academic research and scientific papers
Fluorescent mimetics of CMP-Neu5Ac are highly potent, cell-permeable polarization probes of eukaryotic and bacterial sialyltransferases and inhibit cellular sialylation
Preidl, Johannes J.,Gnanapragassam, Vinayaga S.,Lisurek, Michael,Saupe, J?rn,Horstkorte, Rüdiger,Rademann, J?rg
, p. 5700 - 5705 (2014)
Oligosaccharides of the glycolipids and glycoproteins at the outer membranes of human cells carry terminal neuraminic acids, which are responsible for recognition events and adhesion of cells, bacteria, and virus particles. The synthesis of neuraminic acid containing glycosides is accomplished by intracellular sialyl transferases. Therefore, the chemical manipulation of cellular sialylation could be very important to interfere with cancer development, inflammations, and infections. The development and applications of the first nanomolar fluorescent inhibitors of sialyl transferases are described herein. The obtained carbohydrate-nucleotide mimetics were found to bind all four commercially available and tested eukaryotic and bacterial sialyl transferases in a fluorescence polarization assay. Moreover, it was observed that the anionic mimetics intruded rapidly and efficiently into cells in vesicles and translocated to cellular organelles surrounding the nucleus of CHO cells. The new compounds inhibit cellular sialylation in two cell lines and open new perspectives for investigations of cellular sialylation. You can't run, you can't hide: Sialyltransferases cover cancer cells with neuraminic acids, enabling them to escape from tissues and to metastasize. Cell-permeable chemical probes targeting this class of enzymes might help to study, understand, and inhibit such processes.
A fluorescein-containing, small-molecule, water-soluble receptor for cytosine free bases
Jiang, Yu Lin,Patel, Puneet,Klein, Suzane M.
experimental part, p. 7034 - 7042 (2010/10/21)
In this study, we synthesized small-molecule, water-soluble, fluorescein-containing ureido compounds 6 and 8 as target receptors for cytosine free bases and then investigated the binding of cytosine free bases with the receptors using 15N NMR spectroscopy and partially labeled cytosine-2,4-13C-1,3,4-15N-cytosine. Binding with the receptor 6a (the disodium form of 6) caused the chemical shift of the nitrogen atom of the amino group of cytosine to move downfield; binding of the receptor 8a (the disodium form of 8), which is possessing no corresponding aryl nitrogen atom, had no effect on this signal. Fluorescence spectroscopy revealed that binding of cytosine and its derivatives led to quenching of the fluorescence of receptor 6a; in contrast, the quenching of receptor 8a was only slightly affected by cytosine. Because the fluorescence of 6a was not quenched by either deoxycytidine or uracil, it appears that this receptor is a specific for cytosine among the DNA bases. We used the fluorescence of 6a to measure the apparent binding constants for various cytosine derivatives, including the anticancer prodrug 5-fluorocytosine. Receptor 6a is the first small-molecule, water-soluble fluorescent receptor for the specific binding of cytosine free bases in aqueous solution.
POLYMERASE-INDEPENDENT ANALYSIS OF THE SEQUENCE OF POLYNUCLEOTIDES
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Page/Page column 53, (2008/06/13)
The present invention concerns methods of polymerase independent template directed elongation of polynucleotides, nucleotide building blocks used in these methods as well as the use of the methods and building blocks for the determination of nucleotide sequences, in particular for the determination of SNPs, base modifications, mutations, rearrangements and methylation patterns.
