A promising class of proteomimetics involves brush polymers generated by graft-through living polymerization of peptide-conjugated monomers. The resulting materials, termed protein-like polymers (PLPs), exhibit high proteolytic stability, tunable globularity, efficacy as therapeutic agents, and promise as adhesive materials. Studies of these systems have focused mainly on PLPs composed of disordered peptide monomers, but conformational information on such systems is limited. To obtain greater insight into PLP structure, a library of PLPs of varying lengths were made using structured peptide monomers, including alpha helices, and compared to analogous polymers incorporating a peptide monomer with random coil structure. Circular dichroism spectroscopy confirms the maintenance of the secondary structure of the constituent peptide when polymerized, and small angle X-ray scattering studies inform on the solution-phase conformation of PLPs in different solvent environments. In particular, SAXS studies show that modulation of the hydrophobicity of solvent, as well as the hydrogen bonding patterns of the peptide sidechain, plays an important role in the degree of globularity of the PLP.

Conformational studies of brush polymers of alpha-helical, beta-hairpin, and random coil peptides

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