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Related Experiment Video

Updated: Apr 28, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
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Protein-DNA chimeras for nano assembly.

Diana A Pippig1, Fabian Baumann, Mathias Strackharn

  • 1Center for Nanoscience and Department of Physics, University of Munich , Amalienstraße 54, 80799 Munich, Germany.

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Summary

Researchers developed a new method to attach DNA to proteins, enabling precise molecular assembly for synthetic biology. This technique ensures proteins remain functional during the building process.

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Area of Science:

  • Synthetic Biology
  • Molecular Biology
  • Biochemistry

Background:

Purpose of the Study:

  • Develop a method for site-specific DNA-protein coupling.
  • Arrange protein-DNA chimeras into specific patterns using Single-Molecule Cut & Paste (SMC&P).
  • Verify protein functionality after assembly.

Main Methods:

  • Utilized the ybbR-tag/Sfp enzyme system for covalent attachment of Coenzyme A-modified DNA to Green Fluorescent Protein (GFP).
  • Employed Single-Molecule Cut & Paste (SMC&P) for arranging the resulting DNA-protein chimeras.
  • Monitored protein folding and functionality using fluorescence recordings of individual molecules.

Main Results:

  • Successfully achieved covalent attachment of DNA to GFP with high efficiency and specificity.
  • Demonstrated the ability to arrange DNA-protein chimeras into various patterns via SMC&P.
  • Confirmed that GFP retained its folded structure and full functionality post-assembly.

Conclusions:

  • The ybbR-tag/Sfp system provides a mild, versatile, and robust method for site-specific DNA-protein conjugation.
  • This technique allows for the programmable and selective attachment of DNA handles to proteins.
  • Enables precise spatial organization of proteins for applications in synthetic biology and self-assembly.