ArticleProtein science : a publication of the Protein Society2009
Fusion order controls expression level and activity of elastin-like polypeptide fusion proteins.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 88 citations in OpenAlex.
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Genetic Functionalization of Protein-Based Biomaterials via Protein Fusions.Biomacromolecules · 2024Review
- Understanding the Phase Behavior of a Multistimuli-Responsive Elastin-like Polymer: Insights from Dynamic Light Scattering Analysis.The journal of physical chemistry. B · 2024Article
- Isolation of nucleic acids using liquid-liquid phase separation of pH-sensitive elastin-like polypeptides.Scientific reports · 2024Article
- Engineering synthetic biomolecular condensates.Nature reviews bioengineering · 2023Review
- Improving Biocatalytic Properties of an Azoreductase via the N-Terminal Fusion of Formate Dehydrogenase.Chembiochem : a European journal of chemical biology · 2022Article
- Anti-CD99 scFv-ELP nanoworms for the treatment of acute myeloid leukemia.Nanomedicine : nanotechnology, biology, and medicine · 2020Article
- Anti-FLT3 nanoparticles for acute myeloid leukemia: Preclinical pharmacology and pharmacokinetics.Journal of controlled release : official journal of the Controlled Release Society · 2020Article
- Functional Improvement of Human Cardiotrophin 1 Produced in Tobacco Chloroplasts by Co-expression with Plastid Thioredoxin m.Plants (Basel, Switzerland) · 2020Article
- Incorporation of short, charged peptide tags affects the temperature responsiveness of positively-charged elastin-like polypeptides.Journal of materials chemistry. B · 2019Article
- Unique Phase Transition of Exogenous Fusion Elastin-like Polypeptides in the Solution Containing Polyethylene Glycol.International journal of molecular sciences · 2019Article
- Engineered Ribonucleoprotein Granules Inhibit Translation in Protocells.Molecular cell · 2019Article
- Multifunctional elastin-like polypeptide renders β-glucosidase enzyme phase transition and high stability.Biotechnology for biofuels · 2019Article
- Rapid and simple purification of elastin-like polypeptides directly from whole cells and cell lysates by organic solvent extraction.Biomaterials science · 2018Article
- Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
- Fabricated Elastin.Advanced healthcare materials · 2015Review
- A depot-forming glucagon-like peptide-1 fusion protein reduces blood glucose for five days with a single injection.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
- Elastin-based protein polymer nanoparticles carrying drug at both corona and core suppress tumor growth in vivo.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
- IL-1Ra and its delivery strategies: inserting the association in perspective.Pharmaceutical research · 2013Review
- Predicting transition temperatures of elastin-like polypeptide fusion proteins.Biomacromolecules · 2013Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
We have previously developed a method to purify recombinant proteins, termed inverse transition cycling (ITC) that eliminates the need for column chromatography. ITC exploits the inverse solubility phase transition of an elastin-like polypeptide (ELP) that is fused to a protein of interest. In ITC, a recombinant ELP fusion protein is cycled through its phase transition, resulting in separation of the ELP fusion protein from other Escherichia coli contaminants. Herein, we examine the role of the position of the ELP in the fusion protein on the expression levels and yields of purified protein for four recombinant ELP fusion proteins. Placing the ELP at the C-terminus of the target protein (protein-ELP) results in a higher expression level for the four ELP fusion proteins, which also translates to a greater yield of purified protein. The position of the fusion protein also has a significant impact on its specific activity, as ELP-protein constructs have a lower specific activity than protein-ELP constructs for three out of the four proteins. Our results show no difference in mRNA levels between protein-ELP and ELP-protein fusion constructs. Instead, we suggest two possible explanations for these results: first, the translational efficiency of mRNA may differ between the fusion protein in the two orientations and second, the lower level of protein expression and lower specific activity is consistent with a scenario that placement of the ELP at the N-terminus of the fusion protein increases the fraction of misfolded, and less active conformers, which are also preferentially degraded compared to fusion proteins in which the ELP is present at the C-terminal end of the protein.
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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.