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 mimicLin, Q., Lan, H., Ma, C., Stendall, R. T., Shankland, K., Musgrave, R. A., Horton, P. N., Baldaug, C., Hofmann, H.-J., Butts, C. P., Müller, M. M. and Cobb, A. J. A. (2023) 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. Angewandte Chemie International Edition, 62 (36). e202305326. ISSN 1433-7851
It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1002/anie.202305326 Abstract/SummaryWe 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 alpha- and delta-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 delta-amino acid and the cyclohexyl group of the next delta-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 a-residue functionalities in positions proximal enough to engage in bifunctional catalysis as demonstrated in the application of our system as a minimalist aldolase mimic.
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