Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 144, Issue 35, Pages 15988-15998Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.2c05234
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Funding
- Agence Nationale de la Recherche (ANR) [ANR-17-CE07-0020]
- IdEx Bordeaux [ANR-10-IDEX-03-02]
- program of the French government [ANR-17-CE07-0020]
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education [2021R1A6A3A03040187]
- A Marie Skodowska-Curie postdoctoral fellowship (H2020-MSCA-IF-2014) [661247]
- Agence Nationale de la Recherche (ANR) [ANR-17-CE07-0020] Funding Source: Agence Nationale de la Recherche (ANR)
- National Research Foundation of Korea [2021R1A6A3A03040187] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Marie Curie Actions (MSCA) [661247] Funding Source: Marie Curie Actions (MSCA)
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Amphipathic water-soluble helices formed from synthetic peptides or foldamers are promising building blocks for the creation of self-assembled architectures with non-natural shapes and functions. We have reported a 6-helix bundle that can interact with larger, more complex guest molecules and bind them through an adaptive binding mode.
Amphipathic water-soluble helices formed from synthetic peptides or foldamers are promising building blocks for the creation of self-assembled architectures with non-natural shapes and functions. While rationally designed artificial quaternary structures such as helix bundles have been shown to contain preformed cavities suitable for guest binding, there are no examples of adaptive binding of guest molecules by such assemblies in aqueous conditions. We have previously reported a foldamer 6-helix bundle that contains an internal nonpolar cavity able to bind primary alcohols as guest molecules. Here, we show that this 6-helix bundle can also interact with larger, more complex guests such as n-alkyl glycosides. X-ray diffraction analysis of co-crystals using a diverse set of guests together with solution and gas-phase studies reveals an adaptive binding mode whereby the apo form of the 6-helix bundle undergoes substantial conformational change to accommodate the hydrocarbon chain in a manner reminiscent of glycolipid transfer proteins in which the cavity forms upon lipid uptake. The dynamic nature of the self-assembling and molecular recognition processes reported here marks a step forward in the design of functional proteomimetic molecular assemblies.
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