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Updated: Jan 19, 2026

A Flow Cytometry-Based Cell Surface Protein Binding Assay for Assessing Selectivity and Specificity of an Anticancer Aptamer
Published on: September 13, 2022
Changes in Protein Glycosylation as a Result of Aptamer Interactions with Cancer Cells
Anna Drabik1, Joanna Ner-Kluza1, Kinga Hartman1
1Department of Biochemistry and Neurobiology, Faculty of Materials Science and Ceramics, AGH University of Science and Technology, Krakow, 30-059, Poland.
Purpose:
Based on the recent aptamer-related breast cancer studies, which indicate the therapeutic role of specific oligonucleotide sequences, experiments have been designed in an attempt to unravel the molecular targets of this mechanism. This article describes the study on glycoproteome changes in breast cancer cells as a result of their interactions with aptamers.
Experimental Design:
Aberrations in protein glycosylation play an important role in tumorigenesis and influence cancer progression, metastasis, immunoresponse, and chemoresistance, therefore this study is focused on the identification of the alterations in glycan expression on the surface of proteins as a potential and innovative tool for biomedical applications of aptamers in cancer treatment.
Results:
Two proteins, kinesin-like protein (KI13B) and proliferating cell nuclear antigen (PCNA), have been identified that carry N-glycan epitopes after conjugation with aptamer sequences.
Conclusions And Clinical Relevance:
Multiple features of aptamers as an alternative to protein antibodies are utilized for various biomedical applications ranging from biomarker discovery, bioimaging, targeted therapy, drug delivery, and drug pharmacokinetics and biodistribution. Frequently, aptamers bind to their target molecules and modulate their function. Such therapeutic aptamers can modify the biological pathways for treatment of many types of diseases, such as cancer.
Insights
Researchers identified specific proteins, kinesin-like protein (KI13B) and proliferating cell nuclear antigen (PCNA), that interact with aptamers in breast cancer cells. This finding advances aptamer-based cancer therapy and biomarker discovery.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Aberrant protein glycosylation is crucial in cancer progression and treatment resistance.
- Aptamers offer therapeutic potential in oncology by targeting specific molecular mechanisms.
- Understanding aptamer-target interactions is key for developing novel cancer therapies.
Purpose of the Study:
- To investigate glycoproteome changes in breast cancer cells upon interaction with aptamers.
- To identify molecular targets of aptamer-mediated therapeutic effects in breast cancer.
- To explore aptamers as a tool for biomedical applications in cancer treatment.
Main Methods:
- Studying the interaction between specific aptamer sequences and breast cancer cells.
- Analyzing glycan expression on cell surface proteins.
- Identifying proteins that bind to aptamers and display N-glycan epitopes.
Main Results:
- Two proteins, kinesin-like protein (KI13B) and proliferating cell nuclear antigen (PCNA), were identified.
- These proteins exhibit N-glycan epitopes after conjugation with aptamer sequences.
- This highlights specific molecular targets for aptamer-based breast cancer interventions.
Conclusions:
- Aptamers can be utilized as alternatives to antibodies in various biomedical applications, including cancer therapy.
- The identified proteins (KI13B and PCNA) are potential targets for therapeutic aptamers in breast cancer.
- This research contributes to the development of aptamer-based diagnostics and therapeutics for cancer.
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