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Because cyclic peptides present a benefit of reduced conformational freedom, they have been widely used to mimic the native secondary and tertiary structures of proteins. Although molecular constraint introduced in large cyclic peptides consisting of more than approximately 20 amino acid residues is relatively small, we have found that self-assembly can further constrain these molecules to a significant extent. Over the last decade, we have shown that the self-assembly of large cyclic peptides induces the conformational transition from a random coil to a nearly perfect α-helix, resulting in the formation of highly thermostable, homogeneous and unique molecular nanoscale assemblies. This chapter describes our recent studies on the self-assembly of cyclic and pseudo-cyclic peptides and provides insights into the design and synthesis of self-assembling diblock or triblock cyclic peptides.

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