Sulfation of tyrosine, a common post-translational modification in chemokine receptors, has been shown to enhance binding affinity to multiple chemokine ligands (CCLs). Leveraging this property to address chemokine redundancy, we employed Random Nonstandard Peptides Integrated Discovery mRNA display with genetic code reprogrammingâ´ to generate a library of macrocyclic sulfopeptides incorporating sulfotyrosine. The resulting peptides exhibited broad-spectrum binding to key eosinophil-attracting chemokines: CCL2, CCL7, CCL11, and CCL24.The lead candidate, SP11, demonstrated high affinity for all four ligands and tolerated C-terminal modification for the addition of targeting ligands for therapeutic applications.