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Updated: Apr 5, 2026

A Flow Cytometry-Based Cell Surface Protein Binding Assay for Assessing Selectivity and Specificity of an Anticancer Aptamer
Published on: September 13, 2022
Multimerization of ERBB2/HER2 specific aptamer leads to improved receptor binding.
Georg Mahlknecht1, Ruth Maron2, Bilha Schechter2
1Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel.
This study optimized aptamers for cancer therapy by enhancing their binding affinity and avidity through multimerization. The resulting trimeric aptamer targeting ERBB2/HER2 showed improved efficacy without inducing an immune response in vivo.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Aptamers are emerging as a novel therapeutic strategy for cancer treatment.
- Key aptamer characteristics include specificity and high affinity for target molecules.
Purpose of the Study:
- To elucidate physicochemical parameters of an ERBB2/HER2 specific aptamer.
- To determine the optimal multimerization state for enhanced binding and avidity.
- To assess the immunogenicity of the optimized aptamer.
Main Methods:
- Biochemical assays
- Immunochemical techniques
- Biophysical methodologies
- In vivo studies
Main Results:
- Characterized binding behaviors of multimerized ERBB2/HER2 aptamers.
- Demonstrated structural integrity of multimerized aptamers.
- Confirmed no in vivo immunogenic response for the trimeric aptamer.
Conclusions:
- Multimerization enhances the binding and avidity of ERBB2/HER2 aptamers.
- The trimeric aptamer is a potent and safe therapeutic candidate.
- Developed a methodology to improve aptamer activity for cancer therapy.
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