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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...

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Updated: Jun 5, 2026

Synthetic Condensates and Cell-Like Architectures from Amphiphilic DNA Nanostructures
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Synthetic Condensates and Cell-Like Architectures from Amphiphilic DNA Nanostructures

Published on: May 31, 2024

Assembly of Protein-DNA Framework Nanostructures: Structurally Defining Protein-DNA Interfaces With Aptamer.

Zhe Zhang1,2, Xuanyu Nan3,4, Zhengyu Huang1

  • 1Key Laboratory of Luminescence Analysis and Molecular Sensing (Southwest University), Ministry of Education, College of Pharmaceutical Sciences, Southwest University, Chongqing, China.

Angewandte Chemie (International Ed. in English)
|June 4, 2026
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to create complex protein-DNA frameworks (PDFs) by combining protein-aptamer binding. This advance enables precise control over nanostructure assembly for diverse biomaterial applications.

Keywords:
DNA nanotechnologybiomolecular nanostructuresprotein‐DNA hybrid nanostructuresself‐assembly

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Published on: June 26, 2020

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Structural Biology

Background:

  • Proteins and DNA are used for self-assembling nanostructures, each with unique strengths and weaknesses.
  • Integrating proteins and DNA into protein-DNA frameworks (PDFs) offers potential for diverse structures and functions.
  • Engineering robust protein-DNA interfaces for controlled PDF assembly remains a significant challenge.

Purpose of the Study:

  • To develop a versatile and robust method for engineering protein-DNA interfaces for controlled self-assembly.
  • To demonstrate the creation of diverse protein-DNA frameworks with specific structural and functional properties.

Main Methods:

  • Utilized specific, high-affinity protein-aptamer binding to create controlled interfaces between proteins and DNA.
  • Designed bivalent thrombin aptamers for co-assembly with thrombin.
  • Employed AlphaFold 3 for structural modeling to aid in rational design.
  • Demonstrated versatility using Plasmodium falciparum lactate dehydrogenase (PfLDH).

Main Results:

  • Successfully assembled a range of protein-DNA frameworks (PDFs), including discrete triangles, 3D prisms, linear/circular oligomers, 1D chains/ladders, and 2D arrays.
  • Showcased the strategy's versatility through the assembly of PfLDH-containing PDFs.
  • AlphaFold 3 significantly facilitated structural modeling and design processes.

Conclusions:

  • Developed a rational and versatile approach for designing protein-DNA frameworks (PDFs) via protein-aptamer interfaces.
  • The strategy enables precise control over nanostructure assembly, overcoming previous limitations.
  • These rationally designed PDFs hold promise for multimodal biomaterials integrating protein functionalities and DNA programmability.