ArticlePloS one2011
Crowding alone cannot account for cosolute effect on amyloid aggregation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 69 citations in OpenAlex.
- Article
- Tau Oligomers in Alzheimer's Disease: Modulation Effect of Osmolytes on Amplified Brain-Derived Tau Oligomers.ACS chemical neuroscience · 2025Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Not Always Sticky: Specificity of Protein Stabilization by Sugars Is Conferred by Protein-Water Hydrogen Bonds.Journal of the American Chemical Society · 2023Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Crowding-induced morphological changes in synthetic lipid vesicles determined using smFRET.Frontiers in bioengineering and biotechnology · 2022Article
- Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.Journal of the American Chemical Society · 2021Article
- Osmolytes and crowders regulate aggregation of the cancer-related L106R mutant of the Axin protein.Biophysical journal · 2021Article
- The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding.The Biochemical journal · 2021Article
- Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.QRB discovery · 2021Article
- Self-Assembly of Pseudo-Isocyanine Chloride as a Sensor for Macromolecular Crowding In Vitro and In Vivo.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Properties of Aqueous Trehalose Mixtures: Glass Transition and Hydrogen Bonding.Journal of chemical theory and computation · 2020Article
- Polyols (Glycerol and Ethylene glycol) mediated amorphous aggregate inhibition and secondary structure restoration of metalloproteinase-conalbumin (ovotransferrin).International journal of biological macromolecules · 2017Article
- Effects of hydrophobic macromolecular crowders on amyloid β (16-22) aggregation.Biophysical journal · 2015Article
- Thermodynamics and solvent linkage of macromolecule-ligand interactions.Methods (San Diego, Calif.) · 2015Review
- Effects of macromolecular crowding on amyloid beta (16-22) aggregation using coarse-grained simulations.The journal of physical chemistry. B · 2014Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- The role of crowded physiological environments in prion and prion-like protein aggregation.International journal of molecular sciences · 2013Review
- Quantifying the molecular origins of opposite solvent effects on protein-protein interactions.PLoS computational biology · 2013Article
- Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fiber formation is a specific form of protein aggregation, often resulting from the misfolding of native proteins. Aimed at modeling the crowded environment of the cell, recent experiments showed a reduction in fibrillation halftimes for amyloid-forming peptides in the presence of cosolutes that are preferentially excluded from proteins and peptides. The effect of excluded cosolutes has previously been attributed to the large volume excluded by such inert cellular solutes, sometimes termed "macromolecular crowding". Here, we studied a model peptide that can fold to a stable monomeric β-hairpin conformation, but under certain solution conditions aggregates in the form of amyloid fibrils. Using Circular Dichroism spectroscopy (CD), we found that, in the presence of polyols and polyethylene glycols acting as excluded cosolutes, the monomeric β-hairpin conformation was stabilized with respect to the unfolded state. Stabilization free energy was linear with cosolute concentration, and grew with molecular volume, as would also be predicted by crowding models. After initiating the aggregation process with a pH jump, fibrillation in the presence and absence of cosolutes was followed by ThT fluorescence, transmission electron microscopy, and CD spectroscopy. Polyols (glycerol and sorbitol) increased the lag time for fibril formation and elevated the amount of aggregated peptide at equilibrium, in a cosolute size and concentration dependent manner. However, fibrillation rates remained almost unaffected by a wide range of molecular weights of soluble polyethylene glycols. Our results highlight the importance of other forces beyond the excluded volume interactions responsible for crowding that may contribute to the cosolute effects acting on amyloid formation.
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