ArticleNature communications2024
Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Directed evolution of functional intrinsically disordered proteins.Nature chemical biology · 2026Article
- Biomolecular condensates can function as inherent catalysts.Molecular cell · 2026Article
- A unimolecular GLP-1 and FGF21 dual agonist for treatment of metabolic dysfunction-associated steatohepatitis.Communications medicine · 2026Article
- Catcher Domains as Multifunctional Fusion Modules for Soluble Expression, Covalent Coupling, and Spatial Organization of Recombinant Proteins.Small science · 2026Article
- Review
- AI-aided engineering and production optimization of chimeric hetero-viral capping enzymes for mRNA vaccines.Scientific reports · 2026Article
- Protein-inducible ribosomal frameshifting enables programmable translational control for genetic circuit design in Escherichia coli.Journal of biological engineering · 2026Article
- Two-in-one protein tag enables the soluble expression and calcium-dependent purification of single-chain antibody fragments.Communications biology · 2026Article
- Synthetic Biomolecular Condensates: Design Principles and Applications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A standardized set of pNX vectors for enhanced soluble expression of recombinant proteins in E. coli using small fusion tags.Microbial cell factories · 2025Article
- Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.Applied microbiology and biotechnology · 2025Article
- Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde.Biomolecules · 2025Article
- Nonfouling Coatings from Synthetic Intrinsically Disordered Proteins.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- A Novel Gene Synthesis Platform for Designing Functional Protein Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Effective Gene Expression Prediction and Optimization from Protein Sequences.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Recent advances in recombinant production of soluble proteins in E. coli.Microbial cell factories · 2025Review
- A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025Review
- Injectable microgels containing genetically engineered bacteria for colon cancer therapy through programmed Chemokine expression.Materials today. Bio · 2024Article
- Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.Nature communications · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
We report the de novo design of small (<20 kDa) and highly soluble synthetic intrinsically disordered proteins (SynIDPs) that confer solubility to a fusion partner with minimal effect on the activity of the fused protein. To identify highly soluble SynIDPs, we create a pooled gene-library utilizing a one-pot gene synthesis technology to create a large library of repetitive genes that encode SynIDPs. We identify three small (<20 kDa) and highly soluble SynIDPs from this gene library that lack secondary structure and have high solvation. Recombinant fusion of these SynIDPs to three known inclusion body forming proteins rescue their soluble expression and do not impede the activity of the fusion partner, thereby eliminating the need for removal of the SynIDP tag. These findings highlight the utility of SynIDPs as solubility tags, as they promote the soluble expression of proteins in E. coli and are small, unstructured proteins that minimally interfere with the biological activity of the fused protein.
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