Description:
<jats:p>Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized <jats:bold>CFC</jats:bold> bind to the aromatic peptides <jats:bold>FF</jats:bold> and <jats:bold>YY</jats:bold> (<jats:italic>K</jats:italic> ≈ 229–702 M<jats:sup>−1</jats:sup>), while <jats:bold>AA</jats:bold> binds significantly weaker (<jats:italic>K</jats:italic> ≈ 65–71 M<jats:sup>−1</jats:sup>).</jats:p>