ArticleThe Journal of biological chemistry2014
Heat-induced irreversible denaturation of the camelid single domain VHH antibody is governed by chemical modifications.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Hypervariable loop profiling decodes sequence determinants of antibody stability.Nature structural & molecular biology · 2026Article
- Protein-based Radiopharmaceuticals that target fibroblast activation protein alpha: a review of current progress.EJNMMI radiopharmacy and chemistry · 2025Review
- Improving the production and stability of nanobodies.Protein engineering, design & selection : PEDS · 2025Article
- Designer Small-Molecule Control System Based on Minocycline-Induced Disruption of Protein-Protein Interaction.ACS chemical biology · 2024Article
- Anti-CTLA-4 nanobody as a promising approach in cancer immunotherapy.Cell death & disease · 2024Review
- Site-Specific Structural Changes in Long-Term-Stressed Monoclonal Antibody Revealed with DEPC Covalent-Labeling and Quantitative Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Quantum Cascade Laser Based Infrared Spectroscopy: A New Paradigm for Protein Secondary Structure Measurement.Pharmaceutical research · 2023Article
- A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed inInternational journal of molecular sciences · 2022Article
- An experimental approach probing the conformational transitions and energy landscape of antibodies: a glimmer of hope for reviving lost therapeutic candidates using ionic liquid.Chemical science · 2021Article
- Nanobody-Based Indirect Competitive ELISA for Sensitive Detection of 19-Nortestosterone in Animal Urine.Biomolecules · 2021Article
- Potential False-Positive and False-Negative Results for COVID-19 IgG/IgM Antibody Testing After Heat-Inactivation.Frontiers in medicine · 2020Article
- Anaerobic reduction of europium by a Clostridium strain as a strategy for rare earth biorecovery.Scientific reports · 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
- Mouse Antibody of IgM Class is Prone to Non-Enzymatic Cleavage between CH1 and CH2 Domains.Scientific reports · 2018Article
- Single Domain Antibodies as New Biomarker Detectors.Diagnostics (Basel, Switzerland) · 2017Review
- Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.Scientific reports · 2017Article
- Exploiting sequence and stability information for directing nanobody stability engineering.Biochimica et biophysica acta. General subjects · 2017Article
- Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications.Frontiers in immunology · 2017Review
- Enhancing Stability of Camelid and Shark Single Domain Antibodies: An Overview.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The variable domain of camelid heavy chain antibody (VHH) is highly heat-resistant and is therefore ideal for many applications. Although understanding the process of heat-induced irreversible denaturation is essential to improve the efficacy of VHH, its inactivation mechanism remains unclear. Here, we showed that chemical modifications predominantly governed the irreversible denaturation of VHH at high temperatures. After heat treatment, the activity of VHH was dependent only on the incubation time at 90 °C and was insensitive to the number of heating (90 °C)-cooling (20 °C) cycles, indicating a negligible role for folding/unfolding intermediates on permanent denaturation. The residual activity was independent of concentration; therefore, VHH lost its activity in a unimolecular manner, not by aggregation. A VHH mutant lacking Asn, which is susceptible to chemical modifications, had significantly higher heat resistance than did the wild-type protein, indicating the importance of chemical modifications to VHH denaturation.
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Registered trials
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