Grauer, A. and Riechers, A. and Ritter, S. and König, B. (2008) Synthetic Receptors for the Differentiation of Phosphorylated Peptides with Nanomolar Affinities. Chem. Eur. J. 14, 8922 - 8927.
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Artificial ditopic receptors for the differentiation of phosphorylated peptides varying in i+3 amino acid side chains were synthesized, and their binding affinities and selectivities were determined. The synthetic receptors show the highest binding affinities to phosphorylated peptides under physiological conditions (HEPES, pH 7.5, 154 mM NaCl) reported thus far for artificial systems. The tight and selective binding was achieved by high cooperativity of the two binding moieties in the receptor molecules. All receptors interact with phosphorylated serine by bis(ZnII-cyclen) complex coordination and a second binding site recognizing a carboxylate or imidazole amino acid side chain functionality.
|Institutions:||Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König|
|Projects:||GRK 760, Graduiertenkolleg Medizinische Chemie|
|Keywords:||chelates · cooperativity · emission spectroscopy · molecular recognition · peptides|
|Subjects:||500 Science > 540 Chemistry & allied sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||05 Mar 2009 11:55|
|Last Modified:||08 Nov 2010 13:50|
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