ArticleClinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico2015
Selection of a novel DNA thioaptamer against HER2 structure.
Article in Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Aptamers Targeting Membrane Proteins for Sensor and Diagnostic Applications.Molecules (Basel, Switzerland) · 2023Review
- Breast Cancer Aptamers: Current Sensing Targets, Available Aptamers, and Their Evaluation for Clinical Use in Diagnostics.Cancers · 2021Review
- Selective Anti-melanoma Effect of Phosphothioated Aptamer Encapsulated by Neutral Cytidinyl/Cationic Lipids.Frontiers in cell and developmental biology · 2021Article
- A multifunctional DNA nano-scorpion for highly efficient targeted delivery of mRNA therapeutics.Scientific reports · 2018Article
- Potential Diagnostic and Therapeutic Applications of Oligonucleotide Aptamers in Breast Cancer.International journal of molecular sciences · 2017Review
- Development of Phosphorothioate DNA and DNA Thioaptamers.Biomedicines · 2017Review
- Review
- Improved Aptamers for the Diagnosis and Potential Treatment of HER2-Positive Cancer.Pharmaceuticals (Basel, Switzerland) · 2016Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeHuman epithelial growth factor receptor 2 (HER2) is over-expressed in several malignancies and represents an important therapeutic target. Aptamers are oligonucleotides that may potentially serve as tumor-homing ligand with excellent affinity and specificity for targeted cancer therapy. However, aptamers need to have nuclease resistance in order to function in vivo. The aim of this study was to generate a novel HER2 thioaptamer with enhanced nuclease resistance.
methodsThe HER2 thioaptamer is selected in an evolutionary process called systematic evolution of ligands by exponential enrichment.
resultsThe thioaptamer could bind to the extracellular domain of HER2 with a K d of 172 nM and had minimal cross reactivity to trypsin or IgG. Moreover, the thioaptamer was found capable of binding with the HER2-positive breast cancer cells SK-BR-3 and MDA-MB-453, but not the HER2-negative cells MDA-MB-231. Notably, the thioaptamer HY6 largely maintained its structural integrity facing the nucleases in serum, while regular DNA aptamers were mostly digested. Additionally, the thioaptamer retained the capability of binding with the HER2-positive cells in the presence of serum, whereas non-thionated HER2 aptamer lost the binding function.
conclusionThe results indicated that the selected thioaptamer was more resistant to nuclease than regular DNA aptamers and might potentially function as a HER2-targeting ligand in complicated environment.
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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.