ArticlePloS one2014
Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- TEMPRO: nanobody melting temperature estimation model using protein embeddings.Scientific reports · 2024Article
- Structural and functional characterization of IgG- and non-IgG-based T-cell-engaging bispecific antibodies.Frontiers in immunology · 2024Article
- Quantification of soluble epoxide hydrolase inhibitors in experimental and clinical samples using the nanobody-based ELISA.Journal of pharmaceutical analysis · 2023Article
- NbThermo: a new thermostability database for nanobodies.Database : the journal of biological databases and curation · 2023Article
- Increasing the melting temperature of VHH with the in silico free energy score.Scientific reports · 2023Article
- A novel strategy for developing vaccine candidate against Jaagsiekte sheep retrovirus from the envelope and gag proteins: an in-silico approach.BMC veterinary research · 2022Article
- Structural Insights into the Design of Synthetic Nanobody Libraries.Molecules (Basel, Switzerland) · 2022Review
- Preparation of Specific Nanobodies and Their Application in the Rapid Detection of Nodularin-R in Water Samples.Foods (Basel, Switzerland) · 2021Article
- Nanobody-Based Indirect Competitive ELISA for Sensitive Detection of 19-Nortestosterone in Animal Urine.Biomolecules · 2021Article
- Hyaluronic Acid-Targeted Stimuli-Sensitive Nanomicelles Co-Encapsulating Paclitaxel and Ritonavir to Overcome Multi-Drug Resistance in Metastatic Breast Cancer and Triple-Negative Breast Cancer Cells.International journal of molecular sciences · 2021Article
- A Rationally Designed Bovine IgA Fc Scaffold EnhancesFrontiers in plant science · 2021Article
- Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020Review
- Discrete analysis of camelid variable domains: sequences, structures, and in-silico structure prediction.PeerJ · 2020Article
- Development of a Simple Pretreatment Immunoassay Based on an Organic Solvent-Tolerant Nanobody for the Detection of Carbofuran in Vegetable and Fruit Samples.Biomolecules · 2019Article
- Experimental evaluation of single-domain antibodies predicted by molecular dynamics simulations to have elevated thermal stability.Protein science : a publication of the Protein Society · 2019Article
- Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.Nano letters · 2019Article
- Evaluation of a noncanonical Cys40-Cys55 disulfide linkage for stabilization of single-domain antibodies.Protein science : a publication of the Protein Society · 2019Article
- Analysis of the stability and affinity of BlaR-CTD protein to β-lactam antibiotics based on docking and mutagenesis studies.Journal of biological engineering · 2019Article
- Improvement of antibody affinity by introduction of basic amino acid residues into the framework region.Biochemistry and biophysics reports · 2018Article
- Pairing Alpaca and Llama-Derived Single Domain Antibodies to Enhance Immunoassays for Ricin.Antibodies (Basel, Switzerland) · 2017Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single domain antibodies are the small recombinant variable domains derived from camelid heavy-chain-only antibodies. They are renowned for their stability, in large part due to their ability to refold following thermal or chemical denaturation. In addition to refolding after heat denaturation, A3, a high affinity anti-Staphylococcal Enterotoxin B single domain antibody, possesses a melting temperature of ∼84°C, among the highest reported for a single domain antibody. In this work we utilized the recently described crystal structure of A3 to select locations for the insertion of a second disulfide bond and evaluated the impact that the addition of this second bond had on the melting temperature. Four double-disulfide versions of A3 were constructed and each was found to improve the melting temperature relative to the native structure without reducing affinity. Placement of the disulfide bond at a previously published position between framework regions 2 and 3 yielded the largest improvement (>6°C), suggesting this location is optimal, and seemingly provides a universal route to raise the melting temperature of single domain antibodies. This study further demonstrates that even single domain antibodies with extremely high melting points can be further stabilized by addition of disulfide bonds.
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