ArticleProceedings of the National Academy of Sciences of the United States of America2015
How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 131 citations in OpenAlex.
- Tau Oligomers in Alzheimer's Disease: Modulation Effect of Osmolytes on Amplified Brain-Derived Tau Oligomers.ACS chemical neuroscience · 2025Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants.International journal of molecular sciences · 2024Article
- Effect of Natural Osmolytes on Recombinant Tau Monomer: Propensity of Oligomerization and Aggregation.ACS chemical neuroscience · 2024Article
- Trimethylamine-N-oxide depletes urea in a peptide solvation shell.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multi-scale computer-aided design and photo-controlled macromolecular synthesis boosting uranium harvesting from seawater.Nature communications · 2022Article
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- A Rationalization of the Effect That TMAO, Glycine, and Betaine Exert on the Collapse of Elastin-like Polypeptides.Life (Basel, Switzerland) · 2022Article
- A cosolvent surfactant mechanism affects polymer collapse in miscible good solvents.Communications chemistry · 2020Article
- Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function.Communications biology · 2020Article
- Influence of TMAO as co-solvent on the gelation of silica-PNIPAm core-shell nanogels at intermediate volume fractions.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Nanomechanical properties of steric zipper globular structures.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization.Iranian journal of pharmaceutical research : IJPR · 2019Review
- Preferential Binding of Urea to Single-Stranded DNA Structures: A Molecular Dynamics Study.Biophysical journal · 2018Article
- Mechanism of salt-induced activity enhancement of a marine-derived laccase, Lac15.European biophysics journal : EBJ · 2018Article
- TrimethylamineProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding.Biophysical journal · 2016Article
- TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Biophysical journal · 2016Article
- Folding recombinant spider-silk in H2 O: Effect of osmolytes on the solution conformation of a 15-repeat spider-silk mimetic.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
Abstract
It is currently the consensus belief that protective osmolytes such as trimethylamine N-oxide (TMAO) favor protein folding by being excluded from the vicinity of a protein, whereas denaturing osmolytes such as urea lead to protein unfolding by strongly binding to the surface. Despite there being consensus on how TMAO and urea affect proteins as a whole, very little is known as to their effects on the individual mechanisms responsible for protein structure formation, especially hydrophobic association. In the present study, we use single-molecule atomic force microscopy and molecular dynamics simulations to investigate the effects of TMAO and urea on the unfolding of the hydrophobic homopolymer polystyrene. Incorporated with interfacial energy measurements, our results show that TMAO and urea act on polystyrene as a protectant and a denaturant, respectively, while complying with Tanford-Wyman preferential binding theory. We provide a molecular explanation suggesting that TMAO molecules have a greater thermodynamic binding affinity with the collapsed conformation of polystyrene than with the extended conformation, while the reverse is true for urea molecules. Results presented here from both experiment and simulation are in line with earlier predictions on a model Lennard-Jones polymer while also demonstrating the distinction in the mechanism of osmolyte action between protein and hydrophobic polymer. This marks, to our knowledge, the first experimental observation of TMAO-induced hydrophobic collapse in a ternary aqueous system.
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