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Updated: May 9, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Synthesis and conformational analysis of macrocyclic peptides consisting of both α-helix and polyproline helix
Sung-ju Choi1, Soo hyun Kwon, Tae-Hyun Kim
1Translational Research Center for Protein Function Control and Department of Materials Science & Engineering, Yonsei University, Seoul, 120-749, Korea.
Abstract:
Macrocycles are interesting molecules because their topological features and constrained properties significantly affect their chemical, physical, biological, and self-assembling properties. In this report, we synthesized unique macrocyclic peptides composed of both an α-helix and a polyproline segment and analyzed their conformational properties. We found that the molecular stiffness of the rod-like polyproline segment and the relative orientation of the two different helical segments strongly affect the efficiency of the macrocyclization reaction. Conformational analyses showed that both the α-helix and the polyproline II helix coexisted within the macrocyclic peptides and that the polyproline segment exerts significant effect on the overall helical stability and conformation of the α-helical segment.
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