The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness.

ABSTRACT: The discovery and application of new types of helical peptidic foldamers have been an attractive endeavor to enable the development of new materials, catalysts and biological molecules. To maximize their application potential through structure-based design, it is imperative to control their helical handedness based on their molecular scaffold. Herein we first demonstrate the generalizability of the solid-state right-handed helical propensity of the 4₁₃-helix of L-α/L-sulfono-γ-AA peptides that as short as 11-mer, using the high-resolution X-ray single crystallography. The atomic level folding conformation of the foldamers was also elucidated by 2D NMR and circular dichroism under various conditions. Subsequently, we show that the helical handedness of this class of foldamer is c

SUBMITTER: Teng P 

PROVIDER: S-EPMC9814141 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature