Molecular Stiffening by Macrocycle Clustering

Abstract Allosteric stiffening of a portion of a protein surface is a strategy used in nature to regulate protein oligomerization and provide crucial functions for cells. However, a similar strategy to selectively control part of a compound dynamics remains elusive. Here we show that cucurbit[ n ]uril (CB[ n ]) macrocycles can bind almost all portions of a tetratopic guest molecule, stiffening the different parts of the guest to different extents. “Host–guest” interactions were found to be instrumental in selectively “freezing” guest molecular motions. The combination of 1 H‐NMR (1D, 2D), DOSY, VT‐NMR, isothermal titration calorimetry (ITC), mass spectrometry and molecular modelling enabled to highlight the crucial role of cucurbit[8]uril (CB[8]) binding in the selective hardening of relevant portions of the guest molecule. Beyond implications for bioinspired systems mimicking control of a system dynamic to create a new function, this approach has relevance for improving room temperature phosphorescence, and could also be used to allosterically control organocatalysis in water.

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Publication Details

Journal
Angewandte Chemie
Published
2025-03-25
DOI
https://doi.org/10.1002/ange.202420880
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
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article

Molecular Stiffening by Macrocycle Clustering

Roselyne Rosas, Valérie Monnier, Mehdi Yemloul, Ruibing Wang et al.
Angewandte Chemie
Protein Structure and Dynamics
article

Molecular Stiffening by Macrocycle Clustering

Roselyne Rosas, Valérie Monnier, Mehdi Yemloul, Ruibing Wang, Didier Gigmès, David Bardelang, Stéphane Viel, Anthony Kermagoret, Didier Siri, Laurence Charles, Hang Yin, Qian Cheng
article en

Abstract

Abstract Allosteric stiffening of a portion of a protein surface is a strategy used in nature to regulate protein oligomerization and provide crucial functions for cells. However, a similar strategy to selectively control part of a compound dynamics remains elusive. Here we show that cucurbit[ n ]uril (CB[ n ]) macrocycles can bind almost all portions of a tetratopic guest molecule, stiffening the different parts of the guest to different extents. “Host–guest” interactions were found to be instrumental in selectively “freezing” guest molecular motions. The combination of 1 H‐NMR (1D, 2D), DOSY, VT‐NMR, isothermal titration calorimetry (ITC), mass spectrometry and molecular modelling enabled to highlight the crucial role of cucurbit[8]uril (CB[8]) binding in the selective hardening of relevant portions of the guest molecule. Beyond implications for bioinspired systems mimicking control of a system dynamic to create a new function, this approach has relevance for improving room temperature phosphorescence, and could also be used to allosterically control organocatalysis in water.

Angewandte ChemieVol. 137(22)
Centre National de la Recherche Scientifique (FR), Institut Universitaire de France (FR), University of Macau (MO), Aix-Marseille Université (FR), Institut de Chimie Radicalaire (FR), Centrale Méditerranée (FR)
Clean water and sanitation
Openalex Percentile: Top 95%
Protein Structure and Dynamics
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