ArticlePloS one2015
Single domain antibodies as a powerful tool for high quality surface plasmon resonance studies.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Surface Plasmon Resonance: A Sensitive Tool to Study Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Construction of Synthetic VHH Libraries in Ribosome Display Format.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Light-guided intrabodies for on-demandChemical science · 2021Article
- Direct Immobilization of Engineered Nanobodies on Gold Sensors.ACS applied materials & interfaces · 2021Article
- Influence of nanobody binding on fluorescence emission, mobility, and organization of GFP-tagged proteins.iScience · 2021Article
- Label-Free Biosensors for Laboratory-Based Diagnostics of Infections: Current Achievements and New Trends.Biosensors · 2020Review
- Selectable high-yield recombinant protein production in human cells using a GFP/YFP nanobody affinity support.Protein science : a publication of the Protein Society · 2018Article
- Improving biosensing activity to carcinoembryonic antigen with orientated single domain antibodies.Heliyon · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single domain antibodies are recombinantly expressed functional antibodies devoid of light chains. These binding elements are derived from heavy chain antibodies found in camelids and offer several distinctive properties for applications in biotechnology such as small size, stability, solubility, and expression in high yields. In this study we demonstrated the potential of using single domain antibodies as capturing molecules in biosensing applications. Single domain antibodies raised against green fluorescent protein were anchored onto biosensor surfaces by using several immobilization strategies based on Ni2+:nitrilotriacetic acid-polyhistidine tag, antibody-antigen, biotin-streptavidin interactions and amine-coupling chemistry. The interaction with the specific target of the single domain antibodies was characterized by surface plasmon resonance. The immobilized single domain antibodies show high affinities for their antigens with KD = 3-6 nM and outperform other antibody partners as capturing molecules facilitating also the data analysis. Furthermore they offer high resistance and stability to a wide range of denaturing agents. These unique biophysical properties and the production of novel single domain antibodies against affinity tags make them particularly attractive for use in biosensing and diagnostic assays.
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Registered trials
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.