Peptide-directed microstructure formation of polymers in organic media

Synthesis and peptide-guided self-assembly of an organo-soluble peptide-polymer conjugate, comprising a sequence-defined polypeptide and a poly(n-butyl acrylate), are described. The amino acid sequence of the peptide encodes a high tendency to adopt an antiparallel beta-sheet motif, and thus programs the formation of tapelike microstructures. Easy synthesis and controllable self-assembly is ensured by the incorporation of structure breaking switch defects into the peptide segment. This suppresses temporarily the aggregation tendency of the conjugate as shown by circular dichroism, infrared spectroscopy (FT-IR), and atomic force microscopy (AFM). A pH-controlled rearrangement in the switch segments restores the native peptide backbone, triggering the self-assembly process and leading to the formation of densely twisted tapelike microstructures as could be observed by AFM and transmission electron microscopy. The resulting helical superstructures, when deposited on a substrate, are 2.9 nm high, 10 nm wide, and up to 2.3 mu m long. The helical pitch is about 37 nm, and the pitch angle is 48 degrees. The helical superstructures undergo defined entanglement to form superhelices, leading to the formation of soft, continuous organo-gels. A twisted two-dimensional core-shell tape is proposed as a structure model, in which the peptide segments form anantiparallel beta-sheet with a polymer shell.