ArticleChemical science2020
A bispecific circular aptamer tethering a built-in universal molecular tag for functional protein delivery.
Article in Chemical science, 2020. 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, 24 citations in OpenAlex.
- Structure-guided engineering of an aptamer-PROTAC for targeted degradation of vaccinia-related kinase 1.Chemical science · 2026Article
- Multivalent Aptamers: Contemporary Engineering Strategies and Biomedical Applications.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Green Fluorescent Protein SELEX: Immobilization Chemistry and His-Tag Epitope Bias.Angewandte Chemie (International ed. in English) · 2025Article
- Novel nuclease-resistant RNA aptamer for polyhistidine-tagged proteins and its application in electrochemical aptasensor detection.Biochemistry and biophysics reports · 2025Article
- Facile Splint-Free Circularization of ssDNA with T4 DNA Ligase by Redesigning the Linear Substrate to Form an Intramolecular Dynamic Nick.Biomolecules · 2024Article
- Advances in metal graphitic nanocapsules for biomedicine.Exploration (Beijing, China) · 2022Review
- Optimization of Gonyautoxin1/4-Binding G-Quadruplex Aptamers by Label-Free Surface-Enhanced Raman Spectroscopy.Toxins · 2022Article
- Single-stranded circular DNA theranostics.Theranostics · 2022Review
- Systematic Evolution of Ligands by Exponential Enrichment Technologies and Aptamer-Based Applications: Recent Progress and Challenges in Precision Medicine of Infectious Diseases.Frontiers in bioengineering and biotechnology · 2021Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chemically engineering endogenous amino acids with a molecular tag is one of the most common routes of artificially functionalizing proteins for identification or cellular delivery. However, it is challenging to make conjugation efficient, facile and productive as well as avoiding a high chance of deactivation of the functional proteins. Here we present a new and straightforward design to specifically tether the distinct six polyhistidine tag, terminally expressed on protein cargoes and cellular membrane proteins by using bispecific circular aptamers (bc-apts). The anti-His tag aptamer on one end of the bc-apt can easily recognize the biorthogonal six polyhistidine tag (His tag) on functional proteins like EGFP or RNase A. Meanwhile, a cell-specific aptamer, sgc8, on the other end efficiently facilitates the targeted delivery of functional proteins, improving their overall bioactivity in the cellular milieu by around 4 fold. Therefore, the nuclease-resistant bc-apt is a promising molecular tethering reagent to enable the noncovalent crosslink between live diseased cells and His tag protein cargoes.
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Registered trials
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