ArticleChem2022
Modular Nucleic Acid Scaffolds for Synthesizing Monodisperse and Sequence-Encoded Antibody Oligomers.
Article in Chem, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Assembly of Protein-DNA Framework Nanostructures: Structurally Defining Protein-DNA Interfaces With Aptamer.Angewandte Chemie (International ed. in English) · 2026Article
- Affinity Enhancement in Discrete Multivalent MegaMolecules.Chembiochem : a European journal of chemical biology · 2026Article
- Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026Article
- 33 Unresolved Questions in Nanoscience and Nanotechnology.ACS nano · 2025Article
- The emerging era of structural nanomedicine.Nature reviews bioengineering · 2025Article
- Article
- DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024Article
- Nongenetic surface engineering of mesenchymal stromal cells with polyvalent antibodies to enhance targeting efficiency.Nature communications · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Synthesizing protein oligomers that contain exact numbers of multiple different proteins in defined architectures is challenging. DNA-DNA interactions can be used to program protein assembly into oligomers; however, existing methods require changes to DNA design to achieve different numbers and oligomeric sequences of proteins. Herein, we develop a modular DNA scaffold that uses only six synthetic oligonucleotides to organize proteins into defined oligomers. As a proof-of-concept, model proteins (antibodies) are oligomerized into dimers and trimers, where antibody function is retained. Illustrating the modularity of this technique, dimer and trimer building blocks are then assembled into pentamers containing three different antibodies in an exact stoichiometry and oligomeric sequence. In sum, this report describes a generalizable method for organizing proteins into monodisperse, sequence-encoded oligomers using DNA. This advance will enable studies into how oligomeric protein sequences affect material properties in areas spanning pharmaceutical development, cascade catalysis, synthetic photosynthesis, and membrane transport.
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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.