Synthetic receptors for the differentiation of phosphorylated peptides with nanomolar affinities.
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.
Grauer
Andreas
A
Institute for Organic Chemistry, University of Regensburg, Universitätsstr. 31, 93040 Regensburg (Germany), Fax: (+49) 941-943-1717.
Riechers
Alexander
A
Institute for Organic Chemistry, University of Regensburg, Universitätsstr. 31, 93040 Regensburg (Germany), Fax: (+49) 941-943-1717.
Ritter
Stefan
S
Institute for Organic Chemistry, University of Regensburg, Universitätsstr. 31, 93040 Regensburg (Germany), Fax: (+49) 941-943-1717.
König
Burkhard
B
Institute for Organic Chemistry, University of Regensburg, Universitätsstr. 31, 93040 Regensburg (Germany), Fax: (+49) 941-943-1717.
D015394:Molecular Structure; D010748:Phosphopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017186:Titrimetry
D010748:Phosphopeptides