ArticleJournal of biochemistry2016
The role of intra-domain disulfide bonds in heat-induced irreversible denaturation of camelid single domain VHH antibodies.
Article in Journal of biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
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- Nanobody-based indirect competitive ELISA for the detection of aflatoxin M1 in dairy products.Scientific reports · 2025Article
- A novel sustainable immunoassay for sensitive detection of atrazine based on the anti-idiotypic nanobody and recombinant full-length antibody.Chemical engineering journal (Lausanne, Switzerland : 1996) · 2024Article
- Anti-CTLA-4 nanobody as a promising approach in cancer immunotherapy.Cell death & disease · 2024Review
- Generation of SyntheticACS infectious diseases · 2023Article
- Increasing the melting temperature of VHH with the in silico free energy score.Scientific reports · 2023Article
- Intracellular VHHs to monitor and modulate GPCR signaling.Frontiers in endocrinology · 2022Review
- A Cell-free Expression Pipeline for the Generation and Functional Characterization of Nanobodies.Frontiers in bioengineering and biotechnology · 2022Article
- Nanobodies targeting immune checkpoint molecules for tumor immunotherapy and immunoimaging (Review).International journal of molecular medicine · 2021Review
- Nanobody-Based Indirect Competitive ELISA for Sensitive Detection of 19-Nortestosterone in Animal Urine.Biomolecules · 2021Article
- 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
- Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.Nano letters · 2019Article
- High Expression Achievement of Active and Robust Anti-β2 microglobulin Nanobodies viaMolecules (Basel, Switzerland) · 2019Article
- The structural basis of nanobody unfolding reversibility and thermoresistance.Scientific reports · 2018Article
- Heat denaturation of the antibody, a multi-domain protein.Biophysical reviews · 2018Review
- Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.Scientific reports · 2017Article
- Selection and characterization of specific nanobody against bovine virus diarrhea virus (BVDV) E2 protein.PloS one · 2017Article
- Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Camelid-derived single domain VHH antibodies are highly heat resistant, and the mechanism of heat-induced VHH denaturation predominantly relies on the chemical modification of amino acids. Although chemical modification of disulfide bonds has been recognized as a cause for heat-induced denaturation of many proteins, there have been no mutagenesis studies, in which the number of disulfide bonds was controlled. In this article, we examined a series of mutants of two different VHHs with single, double or no disulfide bonds, and scrutinized the effects of these disulfide bond modifications on VHH denaturation. With the exception of one mutant, the heat resistance of VHHs decreased when the number of disulfide bonds increased. The effect of disulfide bonds on heat denaturation was more striking if the VHH had a second disulfide bond, suggesting that the contribution of disulfide shuffling is significant in proteins with multiple disulfide bonds. Furthermore, our results directly indicate that removal of a disulfide bond can indeed increase the heat resistance of a protein, irrespective of the negative impact on equilibrium thermodynamic stability.
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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.