ArticleBiochimica et biophysica acta. General subjects2017
Exploiting sequence and stability information for directing nanobody stability engineering.
Article in Biochimica et biophysica acta. General subjects, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 65 citations in OpenAlex.
- Nanoscale spatiotemporal cluster analysis of expressed and endogenous proteins.Nature protocols · 2025Review
- Computational Prediction of Single-Domain Immunoglobulin Aggregation Propensities Facilitates Discovery and Humanization of Recombinant Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- Unique mechanisms to increase structural stability and enhance antigen binding in nanobodies.Structure (London, England : 1993) · 2025Article
- Thermodynamic versus kinetic basis for the high conformational stability of nanobodies for therapeutic applications.FEBS letters · 2025Article
- Unveiling the new chapter in nanobody engineering: advances in traditional construction and AI-driven optimization.Journal of nanobiotechnology · 2025Review
- Improving the production and stability of nanobodies.Protein engineering, design & selection : PEDS · 2025Article
- Nanobody-based indirect competitive ELISA for the detection of aflatoxin M1 in dairy products.Scientific reports · 2025Article
- NABP-BERT: NANOBODY®-antigen binding prediction based on bidirectional encoder representations from transformers (BERT) architecture.Briefings in bioinformatics · 2024Article
- A Simple Analysis of the Second (Extra) Disulfide Bridge of VMolecules (Basel, Switzerland) · 2024Article
- TEMPRO: nanobody melting temperature estimation model using protein embeddings.Scientific reports · 2024Article
- A Novel Anti-CD47 Nanobody Tetramer for Cancer Therapy.Antibodies (Basel, Switzerland) · 2024Article
- Development of a synthetic library of humanized nanobodies for targeted IL-6 inhibition.Frontiers in bioengineering and biotechnology · 2024Article
- Structural Insights into the Stability and Recognition Mechanism of the Antiquinalphos Nanobody for the Detection of Quinalphos in Foods.Analytical chemistry · 2023Article
- Generation of SyntheticACS infectious diseases · 2023Article
- NbThermo: a new thermostability database for nanobodies.Database : the journal of biological databases and curation · 2023Article
- Automated optimisation of solubility and conformational stability of antibodies and proteins.Nature communications · 2023Article
- Increasing the melting temperature of VHH with the in silico free energy score.Scientific reports · 2023Article
- NANOBODIES®: A Review of Diagnostic and Therapeutic ApplicationsInternational journal of molecular sciences · 2023Review
- A Novel Cost-Effective Nanobody against Fumonisin B1 Contaminations: Efficacy Test in Dairy Milk and Chickens.Toxins · 2022Article
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
Abstract
backgroundVariable domains of camelid heavy-chain antibodies, commonly named nanobodies, have high biotechnological potential. In view of their broad range of applications in research, diagnostics and therapy, engineering their stability is of particular interest. One important aspect is the improvement of thermostability, because it can have immediate effects on conformational stability, protease resistance and aggregation propensity of the protein.
methodsWe analyzed the sequences and thermostabilities of 78 purified nanobody binders. From this data, potentially stabilizing amino acid variations were identified and studied experimentally.
resultsSome mutations improved the stability of nanobodies by up to 6.1°C, with an average of 2.3°C across eight modified nanobodies. The stabilizing mechanism involves an improvement of both conformational stability and aggregation behavior, explaining the variable degree of stabilization in individual molecules. In some instances, variations predicted to be stabilizing actually led to thermal destabilization of the proteins. The reasons for this contradiction between prediction and experiment were investigated.
conclusionsThe results reveal a mutational strategy to improve the biophysical behavior of nanobody binders and indicate a species-specificity of nanobody architecture. GENERAL SIGNIFICANCE: This study illustrates the potential and limitations of engineering nanobody thermostability by merging sequence information with stability data, an aspect that is becoming increasingly important with the recent development of high-throughput biophysical methods.
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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.