Abiotic ligands that bind to specific biomolecules have attracted attention as substitutes for biomolecular ligands, such as antibodies and aptamers. Radical polymerization enables the production of robust polymeric ligands from inexpensive functional monomers. However, little has been reported about the production of monodispersed polymeric ligands. Herein, we present homogeneous ligands prepared via radical polymerization that recognize epitope sequences on a target peptide and neutralize the toxicity of the peptide. Taking advantage of controlled radical polymerization and separation, a library of multifunctional oligomers with discrete numbers of functional groups was prepared. Affinity screening revealed that the sequence specificity of the oligomer ligands strongly depended on the number of functional groups. The process reported here will become a general step for the development of abiotic ligands that recognize specific peptide sequences.

A series of block oligomers consisting of the same monomer composition but a different block sequence was prepared via reversible addition–fragmentation chain transfer (RAFT) polymerization to screen high affinity ligands for a toxic peptide.

Synthetic polymer nanoparticles (NPs) that recognize and neutralize target biomacromolecules are of considerable interest as "plastic antibodies", synthetic mimics of antibodies. However, monomer sequences in the synthetic NPs are heterogeneous. The heterogeneity limits the target specificity and safety of the NPs. Herein, we report the synthesis of NPs with uniform monomer sequences for recognition and neutralization of target peptides. A multifunctional oligomer with a precise monomer sequence that recognizes the target peptide was prepared via cycles of reversible additionfragmentation chain transfer (RAFT) polymerization and flash chromatography. The oligomer or blend of oligomers was used as a chain transfer agent and introduced into poly(N-isopropyl acrylamide) hydrogel NPs by radical polymerization. Evaluation of the interaction with the peptides revealed that multiple oligomers in NPs cooperatively recognized the sequence of the target peptide and neutralized its toxicity. Effect of sequence, combination, density and molecular weight distribution of precision oligomers on the affinity to the peptides was also investigated.

Synthetic polymer nanoparticles (NPs) that recognize and neutralize target biomacromolecules are of considerable interest as "plastic antibodies", synthetic mimics of antibodies. However, monomer sequences in the synthetic NPs are heterogeneous. The heterogeneity limits the target specificity and safety of the NPs. Herein, we report the synthesis of NPs with uniform monomer sequences for recognition and neutralization of target peptides. A multifunctional oligomer with a precise monomer sequence that recognizes the target peptide was prepared via cycles of reversible additionfragmentation chain transfer (RAFT) polymerization and flash chromatography. The oligomer or blend of oligomers was used as a chain transfer agent and introduced into poly(N-isopropyl acrylamide) hydrogel NPs by radical polymerization. Evaluation of the interaction with the peptides revealed that multiple oligomers in NPs cooperatively recognized the sequence of the target peptide and neutralized its toxicity. Effect of sequence, combination, density and molecular weight distribution of precision oligomers on the affinity to the peptides was also investigated.

Abiotic ligands that bind to specific biomolecules have attracted attention as substitutes for biomolecular ligands, such as antibodies and aptamers. Radical polymerization enables the production of robust polymeric ligands from inexpensive functional monomers. However, little has been reported about the production of monodispersed polymeric ligands. Herein, we present homogeneous ligands prepared via radical polymerization that recognize epitope sequences on a target peptide and neutralize the toxicity of the peptide. Taking advantage of controlled radical polymerization and separation, a library of multifunctional oligomers with discrete numbers of functional groups was prepared. Affinity screening revealed that the sequence specificity of the oligomer ligands strongly depended on the number of functional groups. The process reported here will become a general step for the development of abiotic ligands that recognize specific peptide sequences.