ArticleProtein science : a publication of the Protein Society2017
Understanding the contribution of disulfide bridges to the folding and misfolding of an anti-Aβ scFv.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Two-in-one protein tag enables the soluble expression and calcium-dependent purification of single-chain antibody fragments.Communications biology · 2026Article
- Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Comparative stability and analytical performance of anti-miroestrol recombinant antibody in different cassettes.Applied microbiology and biotechnology · 2023Article
- A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.Nature communications · 2022Article
- Production of Therapeutic Single-Chain Variable Fragments (ScFv) in Pichia pastoris.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Designing and generating a single-chain fragment variable (scFv) antibody against IL2Rα (CD25): AnIranian journal of basic medical sciences · 2021Article
- Application of Antibody Fragments Against Aβ With Emphasis on Combined Application With Nanoparticles in Alzheimer's Disease.Frontiers in pharmacology · 2021Review
- Solubility, Stability, and Avidity of Recombinant Antibody Fragments Expressed in Microorganisms.Frontiers in microbiology · 2020Review
- Production of an anti-Aβ antibody fragment in Pichia pastoris and in vitro and in vivo validation of its therapeutic effect.PloS one · 2017Article
- Effects of an Aβ-antibody fragment on Aβ aggregation and astrocytic uptake are modulated by apolipoprotein E and J mimetic peptides.PloS one · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ScFv-h3D6 is a single chain variable fragment that precludes Aβ peptide-induced cytotoxicity by withdrawing Aβ oligomers from the amyloid pathway to the worm-like pathway. Production of scFv molecules is not a straightforward procedure because of the occurrence of disulfide scrambled conformations generated in the refolding process. Here, we separately removed the disulfide bond of each domain and solved the scrambling problem; and then, we intended to compensate the loss of thermodynamic stability by adding three C-terminal elongation mutations, previously described to stabilize the native fold of scFv-h3D6. Such stabilization occurred through stabilization of the intermediate state in the folding pathway and destabilization of a different, β-rich, intermediate state driving to worm-like fibrils. Elimination of the disulfide bridge of the less stable domain, V
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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.