The solution structures formed by coil–coil copolymers arise from the selective solvation of one of the two blocks and have been well described. In most cases in such relatively simple synthetic structures there are no specific attractive forces that can aid the aggregation process. Nature, however, provides plenty of inspiring polymeric architectures that are shaped and ordered hierarchically by noncovalent forces. The high level of structural definition displayed by proteins, for example, is unmatched by synthetic polymers. An emerging area of interest in polymer science tries to combine the best of both worlds, the natural and the synthetic, by conjugating synthetic polymers and β-sheet-forming peptides. Understanding the supramolecular organization of the block copolymers driven exclusively by the intermolecular attractive forces of the peptide sequence is of particular interest. Not only do these peptide–polymer hybrid structures present an interesting new class of materials, they can also provide important insights into self-organization processes prevalent in nature.
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