Single-molecule force spectroscopy shows that side chain interactions govern the mechanochemical response of polypeptide α-helices and prevent the formation of β-sheets
AFM single-molecule experiments on poly( l -glutamic acid) and poly( l -lysine) show that hydrophobic side chain interactions stabilize α-helices and inhibit the formation of a metastable β-sheet-like structure under mechanical deformation.
Authors
- Sébastien Lecommandoux (ORCID: https://orcid.org/0000-0003-0465-8603)
- Damien Sluysmans (ORCID: https://orcid.org/0000-0002-3462-4407)
- Marie Asano
- Colin V. Bonduelle (ORCID: https://orcid.org/0000-0002-7213-7861)
- Anne‐Sophie Duwez (ORCID: https://orcid.org/0000-0003-1594-2271)
- Nicolas Willet
Institutions
- Centre National de la Recherche Scientifique (FR)
- Université de Bordeaux (FR)
- University of Liège (BE)
- Laboratoire de Chimie des Polymères Organiques (FR)
- Institut Polytechnique de Bordeaux (FR)
Publication Details
- Journal
- RSC Mechanochemistry
- Published
- 2024-08-26
- DOI
- https://doi.org/10.1039/d4mr00068d
- Citations
- 2
- Primary Topic
- Force Microscopy Techniques and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.68
Funders
- Fonds De La Recherche Scientifique - FNRS
- Education, Audiovisual and Culture Executive Agency