Tethering oligopeptides through one end densely packed onto a linear polymer main chain will greatly reduce freedom of the peptide chains, which affords an easy access to investigate the secondary structure of peptides under constrained condition. Herein, molecular brushes with densely grafted monodispersed Cbz-protected oligolysine were efficiently synthesized via free radical polymerization of the macromonomer-bearing lysine octamer, and the secondary structures of the oligopeptide side chains in solutions were investigated. To examine the architecture effects on helical conformation, circular dichroism spectra from the polymer were compared with that from the corresponding macromonomer. To check the chemical structural effects on conformation of the oligopeptide, Cbz groups from the molecular brushes were deprotected, and the secondary structures of the polymers were compared before and after the deprotection. Conformation of the deprotected polymer was further explored by varying solution pH values. Complexation of the positively charged, deprotected polymer with anionic surfactant provides an alternative route to mediate the secondary structures of the short peptides in the constrained environment. It has been found that oligolysine side chains within the molecular brushes can adopt enhanced α-helical conformation through the crowding structures or can form β-sheet by hydrophobic interactions between the complexed surfactants. © 2012 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem, 2012
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