ArticleScientific reports2017
A Systematic Protein Refolding Screen Method using the DGR Approach Reveals that Time and Secondary TSA are Essential Variables.
Article in Scientific reports, 2017. 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, 40 citations in OpenAlex.
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- Nucleases and Their Inhibitors: Exploring Biological Roles, Industrial Applications, and Challenges in Heterologous Expression.Biotechnology journal · 2026Review
- Heterologous expression and foldase-assisted refolding of LipGoM, aBiochemistry and biophysics reports · 2025Article
- Refolding of the recombinant IgV domain of CD47 from E. coli for NMR studies.Protein expression and purification · 2025Article
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- Online monitoring of protein refolding in inclusion body processing using intrinsic fluorescence.Analytical and bioanalytical chemistry · 2024Article
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- Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability.Journal of the American Chemical Society · 2023Article
- Application of biophysical methods for improved protein production and characterization: A case study on an high-temperature requirement A-family bacterial protease.Protein science : a publication of the Protein Society · 2022Article
- A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quality by Design in Downstream Process Development of RomiplostimIranian biomedical journal · 2022Article
- Measuring Protein Aggregation and Stability Using High-Throughput Biophysical Approaches.Frontiers in molecular biosciences · 2022Article
- Application of temperature-responsive HIS-tag fluorophores to differential scanning fluorimetry screening of small molecule libraries.Frontiers in pharmacology · 2022Article
- Nonrefoldability is Pervasive Across theJournal of the American Chemical Society · 2021Article
- Standard operating procedure for fluorescent thermal shift assay (FTSA) for determination of protein-ligand binding and protein stability.European biophysics journal : EBJ · 2021Article
- Selecting Subpopulations of High-Quality Protein Conformers among Conformational Mixtures of Recombinant Bovine MMP-9 Solubilized from Inclusion Bodies.International journal of molecular sciences · 2021Article
- Expression and Refolding of the Plant Chitinase FromFrontiers in bioengineering and biotechnology · 2021Article
- Theory and applications of differential scanning fluorimetry in early-stage drug discovery.Biophysical reviews · 2020Review
- Article
- Improvement of solubility and refolding of an anti-human epidermal growth factor receptor 2 single-chain antibody fragment inclusion bodies.Research in pharmaceutical sciences · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Refolding of proteins derived from inclusion bodies is very promising as it can provide a reliable source of target proteins of high purity. However, inclusion body-based protein production is often limited by the lack of techniques for the detection of correctly refolded protein. Thus, the selection of the refolding conditions is mostly achieved using trial and error approaches and is thus a time-consuming process. In this study, we use the latest developments in the differential scanning fluorimetry guided refolding approach as an analytical method to detect correctly refolded protein. We describe a systematic buffer screen that contains a 96-well primary pH-refolding screen in conjunction with a secondary additive screen. Our research demonstrates that this approach could be applied for determining refolding conditions for several proteins. In addition, it revealed which "helper" molecules, such as arginine and additives are essential. Four different proteins: HA-RBD, MDM2, IL-17A and PD-L1 were used to validate our refolding approach. Our systematic protocol evaluates the impact of the "helper" molecules, the pH, buffer system and time on the protein refolding process in a high-throughput fashion. Finally, we demonstrate that refolding time and a secondary thermal shift assay buffer screen are critical factors for improving refolding efficiency.
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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.