ArticleBiophysical journal2012
A desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 38 citations in OpenAlex.
- Optimizing the synthesis of dimeric peptides: influence of the reaction medium and effects that modulate kinetics and reaction yield.Amino acids · 2023Article
- Trifluoroethanol and the behavior of a tardigrade desiccation-tolerance protein.Protein science : a publication of the Protein Society · 2023Article
- Progressive Phosphorylation Modulates the Self-Association of a Variably Modified Histone H3 Peptide.Frontiers in molecular biosciences · 2021Article
- The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates.Chemical science · 2020Article
- Protein Environment: A Crucial Triggering Factor in Josephin Domain Aggregation: The Role of 2,2,2-Trifluoroethanol.International journal of molecular sciences · 2018Article
- Experimental validation of the role of trifluoroethanol as a nanocrowder.The journal of physical chemistry. B · 2014Article
- Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain.International journal of molecular sciences · 2013Article
- Inhibition of ovine in vitro fertilization by anti-Prt antibody: hypothetical model for Prt/ZP interaction.Reproductive biology and endocrinology : RB&E · 2013Article
- Structural basis of fluorescence quenching in caspase activatable-GFP.Protein science : a publication of the Protein Society · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Studies of amyloid disease-associated proteins in aqueous solutions containing 2,2,2-trifluoroethanol (TFE) have shown that the formation of structural intermediates is often correlated with enhanced protein aggregation. Here, enhanced green fluorescent protein (EGFP) is used as a model protein system to investigate the causal relationship between TFE-induced structural transitions and aggregation. Using circular dichroism spectroscopy, light scattering measurements, and transmission electron microscopy imaging, we demonstrate that population of a partially α-helical, monomeric intermediate is roughly correlated with the growth of β-sheet-rich, flexible fibrils for acid-denatured EGFP. By fitting our circular dichroism data to a model in which TFE-water mixtures are assumed to be ideal solutions, we show that increasing entropic costs of protein solvation in TFE-water mixtures may both cause the population of the intermediate state and increase aggregate production. Tertiary structure and electrostatic repulsion also impede aggregation. We conclude that initiation of EGFP aggregation in TFE likely involves overcoming of multiple protective factors, rather than stabilization of aggregation-prone structural elements.
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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.