DEVAUX, Floriane; LI, Xuesong; SLUYSMANS, Damien; MAURIZOT, Victor; BAKALIS, Evangelos; ZERBETTO, Francesco; HUC, Ivan; DUWEZ, Anne-Sophie

doi:10.1016/j.chempr.2021.02.030

Métadonnées

Afficher la notice complète

Licence d’utilisation du document

DEVAUX, Floriane
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

LI, Xuesong
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

SLUYSMANS, Damien

Langue

Article de revue

Ce document a été publié dans

Chem. 2021-05, vol. 7, n° 5, p. 1333-1346

Résumé en anglais

Because of proteins’ many degrees of conformational freedom, programming protein folding dynamics, overall elasticity, and motor functions remains an elusive objective. Instead, smaller and simpler objects, such as synthetic foldamers, may be amenable to design. However, little is known about their mechanical performance. Here, we show that reducing molecular size may not compromise mechanical properties. We report that helical aromatic oligoamides as small as 1 nm possess outstanding elasticity and outperform most natural helices. Using single-molecule force spectroscopy, we characterize their folding trajectories and intermediate states. We show that they cooperatively and reversibly unwind at high forces. They extend up to 3.8 times their original length and rewind against considerable forces on a timescale of 10 μs. Pulling and relaxing cycles follow the same trace up to a very high loading rate, indicating that the mechanical energy accumulated during the stretching does not dissipate and is immediately reusable.< Réduire

Mots clés en anglais

foldamers

helical folding

AFM force spectroscopy

single-molecule mechanics

elasticity

reversible processes

molecular machines with tailored properties

Projet Européen

Beyond Biopolymers: Protein-Sized Aromatic Amide Functional Foldamers
Erasmus Mundus - International Doctoral School in Functional Materials

Unités de recherche

CBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248