Abstract

Aromatic oligomers constitute a distinct and promising class of synthetic foldamers – oligomers that adopt stable folded conformations. Single helical structures are, to a large extent, predictable, show unprecedented conformational stability, and represent convenient building blocks to elaborate synthetic, very large (protein-sized) folded architectures. This lecture will give an overview of our current efforts to design abiotic tertiary structures based on aromatic scaffolds,[1] to prepare and select (as opposed to design) aromatic foldamer-peptide hybrid architectures,[2,3] and to use aromatic foldamers to recognize sizeable protein surfaces.[4,5]

References:

[1] S. De et al., Designing cooperatively folded abiotic uni- and multimolecular helix bundles, Nat. Chem. 2018, 10, 51. [2] J. M. Rogers, S. Kwon et al. Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids, Nat. Chem. 2018, 10, 405. [3] M. Kudo, V. Maurizot, B. Kauffmann, A. Tanatani, I. Huc, Folding of a linear array of a-amino acids within a helical aromatic oligoamide frame, J. Am. Chem. Soc. 2013, 135, 9628. [4] K. Ziach, C. Chollet, et al., Single helically folded aromatic oligoamides that mimic the charge surface of double-stranded B-DNA, Nat. Chem. 2018, 10, 511. [5] M. Jewginski, T. Granier, B. Langlois d’Estaintot, L. Fischer, C. D. Mackereth, I. Huc, Self-assembled protein-aromatic foldamer complexes with 2:3 and 2:2:1 stoichiometries, J. Am. Chem. Soc. 2017, 139, 2928