ArticleAngewandte Chemie (International ed. in English)2018
Conformationally Programmable Chiral Foldamers with Compact and Extended Domains Controlled by Monomer Structure.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Boost of Chiroptical Responses Through the Enhancement of Electron Transition Dipole Moment.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Non-Covalent Interactions Enforce Conformation in Switchable and Water-Soluble Diketopiperazine-Pyridine Foldamers.Angewandte Chemie (International ed. in English) · 2023Article
- A spirocyclic backbone accesses new conformational space in an extended, dipole-stabilized foldamer.Communications chemistry · 2023Article
- Chiral, sequence-definable foldamer-derived macrocycles.Chemical science · 2021Article
- Conformationally Programmable Chiral Foldamers with Compact and Extended Domains Controlled by Monomer Structure.Angewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
Foldamers are an important class of abiotic macromolecules, with potential therapeutic applications in the disruption of protein-protein interactions. The majority adopt a single conformational motif such as a helix. A class of foldamer is now introduced where the choice of heterocycle within each monomer, coupled with a strong conformation-determining dipole repulsion effect, allows both helical and extended conformations to be selected. Combining these monomers into hetero-oligomers enables highly controlled exploration of conformational space and projection of side-chains along multiple vectors. The foldamers were rapidly constructed via an iterative deprotection-cross-coupling sequence, and their solid- and solution-phase conformations were analysed by X-ray crystallography and NMR and CD spectroscopy. These molecules may find applications in protein surface recognition where the interface does not involve canonical peptide secondary structures.
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