ORGN 633 |
| We report a new highly chemoselective reaction that proceeds in an aqueous buffer tolerating the presence of a wide variety of amino acids including lysine. This reaction is between a cysteine or the N-terminus cysteine of a peptide and a modified squarate moiety. We will present our working hypothesis of a molecular lock mechanism, which guided us to fine-tune of the squarate derivatives to achieve high selectivity with quantitative yield in aqueous buffer. In contrast to the reaction of maleimide-thiol coupling, our reaction can tolerate the presence of an internal cysteine within a peptide, and thus provides a means to expand the scope peptide immobilization methodology. Furthermore, the squarate substrate is not degraded by the key relevant enzymes from cells. We will present our on-going exploration of using this ligation in a living mammalian cell to interrogate difficult cell signaling pathways involving glycosylation. |
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Proteins, Peptides, Amino Acids, and Enzyme Inhibitors
8:00 AM-12:00 PM, Thursday, 30 March 2006 Georgia World Congress Center -- C301, Oral
Division of Organic Chemistry |