In solution, foldamers adopt preferred secondary structures that almost exclusively consist of various helix or sheet types. In biomacromolecules, such as proteins, these secondary structural motifs can further be organized into higher order structures using covalent loops, i.e. tertiary structures, and even further using noncovalent interactions between subunits, i.e. quaternary structures. At interfaces, however, both the conformational preference of the foldamer and the intermolecular interactions between individual foldamer strands might be largely altered (Fig. 13.2). Several examples from the literature (see below) show such behavior.
Was this article helpful?