Experimental study demonstrates α-helix stabilization in short cyclic peptides, indicating a novel strategy for designing directional self-assembled nanomaterials.
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.
No takes yet. Share an insight, caveat, or question.
Sim et al. (2012) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: