title: Synthesis and conformational analysis of macrocyclic peptides consisting of both α-helix and polyproline helix segments.
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.
authors.affiliation: Translational Research Center for Protein Function Control and Department of Materials Science & Engineering, Yonsei University, Seoul, 120-749, Korea.
authors.forename: Sung-ju
authors.initials: SJ
authors.lastname: Choi
authors.forename: Soo hyun
authors.initials: Sh
authors.lastname: Kwon
authors.forename: Tae-Hyun
authors.initials: TH
authors.lastname: Kim
authors.forename: Yong-beom
authors.initials: YB
authors.lastname: Lim
mesh_terms: D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides
keywords: macrocycles; peptides; polyproline; α-helix