ArticleAnalytical and bioanalytical chemistry2017
Characterization of the specific interaction between the DNA aptamer sgc8c and protein tyrosine kinase-7 receptors at the surface of T-cells by biosensing AFM.
Article in Analytical and bioanalytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 39 citations in OpenAlex.
- Atomic Force Microscopy Based Single Molecule Recognition: Deciphering Biological Interactions at the Nanoscale.Journal of molecular recognition : JMR · 2026Review
- Aptamer-based approaches in leukemia: a paradigm shift in targeted therapy.Clinical and experimental medicine · 2025Review
- Nanotechnology-based diagnostics and therapeutics in acute lymphoblastic leukemia: a systematic review of preclinical studies.Nanoscale advances · 2023Review
- Advances in aptamer-based nuclear imaging.European journal of nuclear medicine and molecular imaging · 2022Review
- In Vivo Evaluation of Sgc8-c Aptamer as a Molecular Imaging Probe for Colon Cancer in a Mouse Xenograft Model.International journal of molecular sciences · 2022Article
- Recent advances in understanding oligonucleotide aptamers and their applications as therapeutic agents.3 Biotech · 2020Review
- Current Perspectives on Aptamers as Diagnostic Tools and Therapeutic Agents.Pharmaceutics · 2020Review
- Control of Ligand-Binding Specificity Using Photocleavable Linkers in AFM Force Spectroscopy.Nano letters · 2020Article
- Nucleic Acid Aptamer: A Novel Potential Diagnostic and Therapeutic Tool for Leukemia.OncoTargets and therapy · 2019Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied the interaction of the specific DNA aptamer sgc8c immobilized at the AFM tip with its corresponding receptor, the protein tyrosine kinase-7 (PTK7) embedded in the membrane of acute lymphoblastic leukemia (ALL) cells (Jurkat T-cells). Performing single molecule force spectroscopy (SMFS) experiments, we showed that the aptamer sgc8c bound with high probability (38.3 ± 7.48%) and high specificity to PTK7, as demonstrated by receptor blocking experiments and through comparison with the binding behavior of a nonspecific aptamer. The determined kinetic off-rate (k
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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.