ArticleNucleic acids research2003
A DNA Spiegelmer to staphylococcal enterotoxin B.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Fluorescent aptasensor targeting the fibrinogen-binding domain of clumping factor A for rapid detection of Staphylococcus aureus.Mikrochimica acta · 2026Article
- Integrating FRET and Molecular Dynamics Simulation for Single-Molecule Aptameric Detection of Staphylococcus aureus IsdA Surface Protein.Biotechnology journal · 2025Article
- Enhanced SELEX Platforms for Aptamer Selection with Improved Characteristics: A Review.Molecular biotechnology · 2025Review
- Staphylococcal Enterotoxins: Description and Importance in Food.Pathogens (Basel, Switzerland) · 2024Review
- Screening of Single-Stranded DNA Aptamer Specific for Florfenicol and Application in Detection of Food Safety.Biosensors · 2022Article
- [Preparation of dual-functional composite magnetic nanomaterials modified with different metals/aptamers and their performance in exosome enrichment].Se pu = Chinese journal of chromatography · 2021Article
- Spiegelmer-Based Sandwich Assay for Cardiac Troponin I Detection.International journal of molecular sciences · 2020Article
- Aptamers, the Nucleic Acid Antibodies, in Cancer Therapy.International journal of molecular sciences · 2020Review
- Aptamers Chemistry: Chemical Modifications and Conjugation Strategies.Molecules (Basel, Switzerland) · 2019Review
- Chemical Modifications of Nucleic Acid Aptamers for Therapeutic Purposes.International journal of molecular sciences · 2017Review
- Adaptive PCR Based on Hybridization Sensing of Mirror-Image l-DNA.Analytical chemistry · 2017Article
- In vitro evolution of chemically-modified nucleic acid aptamers: Pros and cons, and comprehensive selection strategies.RNA biology · 2016Review
- Molecular Selection, Modification and Development of Therapeutic Oligonucleotide Aptamers.International journal of molecular sciences · 2016Review
- Biostable L-DNAzyme for Sensing of Metal Ions in Biological Systems.Analytical chemistry · 2016Article
- A novel IgY-Aptamer hybrid system for cost-effective detection of SEB and its evaluation on food and clinical samples.Scientific reports · 2015Article
- Neutralization of staphylococcal enterotoxin B by an aptamer antagonist.Antimicrobial agents and chemotherapy · 2015Article
- Selecting Molecular Recognition. What Can Existing Aptamers Tell Us about Their Inherent Recognition Capabilities and Modes of Interaction?Pharmaceuticals (Basel, Switzerland) · 2012Article
- A single-stranded DNA aptamer that selectively binds to Staphylococcus aureus enterotoxin B.PloS one · 2012Article
- Aptamers as therapeutics.Nature reviews. Drug discovery · 2010Review
- Mirror image DNA nanostructures for chiral supramolecular assemblies.Nano letters · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial staphylococcal enterotoxin B is involved in several severe disease patterns and it was therefore used as a target for the generation of biologically stable mirror-image oligonucleotide ligands, so called Spiegelmers. The toxin is a 28 kDa protein consisting of 239 amino acids. Since the full-length protein is not accessible to chemical peptide synthesis, a stable domain of 25 amino acids was identified as a suitable selection target. DNA in vitro selection experiments were carried out against the equivalent mirror-image D-peptide domain resulting in high affinity D-DNA aptamers. As expected, the corresponding enantiomeric L-DNA Spiegelmer showed comparable binding characteristics to the L-peptide domain. Moreover, the Spiegelmer bound the whole protein target with only slightly reduced affinity. Dissociation constants of both peptide-oligonucleotide complexes were measured in the range of 200 nM, whereas the Spiegelmer binding to the full-length protein was determined at approximately 420 nM. These data demonstrate the possibility to identify Spiegelmers against large protein targets by a domain approach.
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