Crystal Structure and NMR of an α,δ-Peptide Foldamer Helix Shows Side-Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic

Qi Lin, Hao Lan, Chunmiao Ma, Ryan T Stendall, Kenneth Shankland, Rebecca A Musgrave, Peter N Horton, Carsten Baldauf, Hans-Jörg Hofmann, Craig P Butts, Manuel M Müller, Alexander J A Cobb*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

We report the first NMR and X-ray diffraction (XRD) structures of an unusual 13/11-helix (alternating i, i+1 {NH-O=C} and i, i+3 {C=O-H-N} H-bonds) formed by a heteromeric 1 : 1 sequence of α- and δ-amino acids, and demonstrate the application of this framework towards catalysis. Whilst intramolecular hydrogen bonds (IMHBs) are the clear driver of helix formation in this system, we also observe an apolar interaction between the ethyl residue of one δ-amino acid and the cyclohexyl group of the next δ-residue in the sequence that seems to stabilize one type of helix over another. To the best of our knowledge this type of additional stabilization leading to a specific helical preference has not been observed before. Critically, the helix type realized places the α-residue functionalities in positions proximal enough to engage in bifunctional catalysis as demonstrated in the application of our system as a minimalist aldolase mimic.

Original languageEnglish
Article numbere202305326
JournalANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume62
Issue number36
Early online date23 May 2023
DOIs
Publication statusPublished - 4 Sept 2023

Fingerprint

Dive into the research topics of 'Crystal Structure and NMR of an α,δ-Peptide Foldamer Helix Shows Side-Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic'. Together they form a unique fingerprint.

Cite this