ArticleBiochemistry2015
Chemical Interactions of Polyethylene Glycols (PEGs) and Glycerol with Protein Functional Groups: Applications to Effects of PEG and Glycerol on Protein Processes.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 120 citations in OpenAlex.
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- Crowding beyond excluded volume: A tale of two dimers.Protein science : a publication of the Protein Society · 2025Article
- PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025Article
- Synthesis and In Vitro Antileishmanial Efficacy of Novel Ethylene Glycol Analogues of Benzothiadiazine-1,1-dioxide.Chemistry & biodiversity · 2025Article
- The molecular basis for hydrodynamic properties of PEGylated human serum albumin.Biophysical journal · 2024Article
- Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin.Biophysical journal · 2024Article
- Diffusiophoresis in Polymer and Nanoparticle Gradients.The journal of physical chemistry. B · 2024Article
- Striving for Uniformity: A Review on Advances and Challenges To Achieve Uniform Polyethylene Glycol.Organic process research & development · 2024Review
- Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.Nature communications · 2023Article
- Quantifying Amide-Aromatic Interactions at Molecular and Atomic Levels: Experimentally-determined Enthalpic and Entropic Contributions to Interactions of Amide spbioRxiv : the preprint server for biology · 2023Article
- Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail.The journal of physical chemistry. B · 2023Article
- Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding.Biomolecules · 2023Article
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein.Journal of molecular biology · 2022Article
- Ion Complexation Explains Orders of Magnitude Changes in the Equilibrium Constant of Biochemical Reactions in Buffers Crowded by Nonionic Compounds.The journal of physical chemistry letters · 2022Article
- Hydroxylation of pregnenolone and dehydroepiandrosterone by zygomycete Backusella lamprospora VKM F-944: selective production of 7α-OH-DHEA.Applied microbiology and biotechnology · 2022Article
- Weakly hydrated anions bind to polymers but not monomers in aqueous solutions.Nature chemistry · 2022Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
In this work, we obtain the data needed to predict chemical interactions of polyethylene glycols (PEGs) and glycerol with proteins and related organic compounds and thereby interpret or predict chemical effects of PEGs on protein processes. To accomplish this, we determine interactions of glycerol and tetraEG with >30 model compounds displaying the major C, N, and O functional groups of proteins. Analysis of these data yields coefficients (α values) that quantify interactions of glycerol, tetraEG, and PEG end (-CH2OH) and interior (-CH2OCH2-) groups with these groups, relative to interactions with water. TetraEG (strongly) and glycerol (weakly) interact favorably with aromatic C, amide N, and cationic N, but unfavorably with amide O, carboxylate O, and salt ions. Strongly unfavorable O and salt anion interactions help make both small and large PEGs effective protein precipitants. Interactions of tetraEG and PEG interior groups with aliphatic C are quite favorable, while interactions of glycerol and PEG end groups with aliphatic C are not. Hence, tetraEG and PEG300 favor unfolding of the DNA-binding domain of lac repressor (lacDBD), while glycerol and di- and monoethylene glycol are stabilizers. Favorable interactions with aromatic and aliphatic C explain why PEG400 greatly increases the solubility of aromatic hydrocarbons and steroids. PEG400-steroid interactions are unusually favorable, presumably because of simultaneous interactions of multiple PEG interior groups with the fused ring system of the steroid. Using α values reported here, chemical contributions to PEG m-values can be predicted or interpreted in terms of changes in water-accessible surface area (ΔASA) and separated from excluded volume effects.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.