Synthetic Receptors for the Differentiation of Phosphorylated Peptides with Nanomolar Affinities

Grauer, Andreas and Riechers, Alexander and Ritter, Stefan and Koenig, Burkhard (2008) Synthetic Receptors for the Differentiation of Phosphorylated Peptides with Nanomolar Affinities. CHEMISTRY-A EUROPEAN JOURNAL, 14 (29). pp. 8922-8927. ISSN 0947-6539, 1521-3765

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Abstract

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(Zn-II-cyclen) complex coordination and a second binding site recognizing a carboxylate or imidazole amino acid side chain functionality.

Item Type: Article
Uncontrolled Keywords: PROTEIN-KINASE ACTIVITY; POLYACRYLAMIDE-GEL ELECTROPHORESIS; MOLECULAR RECOGNITION; AQUEOUS-SOLUTION; ARTIFICIAL RECEPTORS; SELECTIVE RECOGNITION; GUANIDINIUM CATIONS; CARBOXYLATE BINDING; SIGNAL-TRANSDUCTION; LIVING CELLS; chelates; cooperativity; emission spectroscopy; molecular recognition; peptides
Subjects: 500 Science > 540 Chemistry & allied sciences
Divisions: Chemistry and Pharmacy > Institut für Organische Chemie
Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König
Depositing User: Dr. Gernot Deinzer
Date Deposited: 11 Nov 2020 10:06
Last Modified: 11 Nov 2020 10:06
URI: https://pred.uni-regensburg.de/id/eprint/31585

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