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Directional Assembly of α-Helical Peptides Induced by Cyclization
- Sim, Seunghyun, Kim, Yongju, Kim, Taehoon, Lim, Sunhee, Lee, Myongsoo
- Journal of the American Chemical Society 2012 v.134 no.50 pp. 20270-20272
- cyclic peptides, hydrophobicity, methodology, micelles, nanofibers, protein secondary structure
- Effective stabilization of short peptide chains into a helical structure has been a challenge in the fields of chemistry and biology. Here we report a novel method for α-helix stabilization of short peptides through their confinement in a cyclic architecture. We synthesized block peptides based on a short peptide and a flexible linker as linear precursors. Subsequent cyclization of the peptide precursors resulted in a conformational change of the peptide unit from a random coil to an α-helix. The incorporation of hydrophobic residues into the peptide unit led to a facially amphiphilic conformation of the molecular cycle. The resulting amphiphilic peptide self-assembled into undulated nanofibers through the directional assembly of small oblate micelles.