Simple Structural Requirements for Sequence-Selective Peptide Receptors? Tripeptide Binding by a Podand Ionophore

Abstract

A simple, dye(R)-labeled and conformationally restricted ionophore 2 was prepared and screened for peptide binding using solid-supported combinatorial libraries of 24 389 protected and unprotected tripeptides. The ionophore was found generally to bind unhindered cationic peptides having arginines or N-terminal glycines. The podand was particularly selective in the case of unprotected tripeptides and was able to selectively bind a single tripeptide (l-Arg-l-Phe-d-Asp) from the unprotected ∼24000-member tripeptide library. These results indicate that relatively simple organic molecules can make highly sequence-selective receptors for tripeptides. Structural features of such receptors are discussed.

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