ArticleNano letters2020
Influence of Fluorination on Single-Molecule Unfolding and Rupture Pathways of a Mechanostable Protein Adhesion Complex.
Article in Nano letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- A Physics-Augmented Deep Learning Framework for Classifying Single Molecule Force Spectroscopy Data.Proceedings of machine learning research · 2025Article
- Engineering the Mechanical Stability of a Therapeutic Affibody/PD-L1 Complex by Anchor Point Selection.bioRxiv : the preprint server for biology · 2024Article
- Anisotropic Friction in a Ligand-Protein Complex.Nano letters · 2023Article
- Fluorine-Containing Drug Administration in Rats Results in Fluorination of Selected Proteins in Liver and Brain Tissue.International journal of molecular sciences · 2022Article
- Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022Review
- Facile Synthesis of Peptide-Conjugated Gold Nanoclusters with Different Lengths.Nanomaterials (Basel, Switzerland) · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Control of NanoscaleACS nano · 2021Article
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Authors and funding
5 authors.
Funding
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Abstract
We investigated the influence of fluorination on unfolding and unbinding reaction pathways of a mechanostable protein complex comprising the tandem dyad XModule-Dockerin bound to Cohesin. Using single-molecule atomic force spectroscopy, we mapped the energy landscapes governing the unfolding and unbinding reactions. We then used sense codon suppression to substitute trifluoroleucine in place of canonical leucine globally in XMod-Doc. Although TFL substitution thermally destabilized XMod-Doc, it had little effect on XMod-Doc:Coh binding affinity at equilibrium. When we mechanically dissociated global TFL-substituted XMod-Doc from Coh, we observed the emergence of a new unbinding pathway with a lower energy barrier. Counterintuitively, when fluorination was restricted to Doc, we observed mechano-stabilization of the non-fluorinated neighboring XMod domain. This suggests that intramolecular deformation is modulated by fluorination and highlights the differences between equilibrium thermostability and non-equilibrium mechanostability. Future work is poised to investigate fluorination as a means to modulate mechanical properties of synthetic proteins and hydrogels.
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