Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

Unique folded structures of natural and synthetic oligomers are the most fundamental basis for their unique functions. N-Substituted β-peptides, or β-peptoids, are synthetic oligomers with great potential to fold into diverse three-dimensional structures because of the existence of four rotatable bonds in a monomer with highly modular synthetic accessibility. However, the existence of the four rotatable bonds poses a challenge for conformational control of β-peptoids. Here, we report a strategy for per-residue programming of two dihedral angles of β-peptoids, which is useful for restricting the conformational space of the oligomers. The oligomer was found to form a unique loop conformation that is stabilized by the backbone rotational restrictions. Circular dichroism and NMR spectroscopic analyses and X-ray crystallographic analysis of the oligomer are presented. The strategy would significantly facilitate the discovery of many more unique folded structures of β-peptoids.


Jumpei Morimoto, Jungyeon Kim, Daisuke Kuroda, Satoru Nagatoishi, Kouhei Tsumoto, Shinsuke Sando. Per-Residue Program of Multiple Backbone Dihedral Angles of β-Peptoids via Backbone Substitutions. Journal of the American Chemical Society. 2020 Feb 05;142(5):2277-2284

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 31917919

View Full Text