Related Experiment Video
Updated: Jul 12, 2025
07:44
Design and Synthesis of a Reconfigurable DNA Accordion Rack
Published on: August 15, 2018
7.1K
Light-Activated Assembly of DNA Origami into Dissipative Fibrils
Willi R Berg1,2, Jonathan F Berengut3,4, Changzhuang Bai1
1School of Chemistry, University of New South Wales, Sydney, 2052, Australia.
Angewandte Chemie (International Ed. in English)
|October 30, 2023
Summary
Researchers created dynamic, micron-length DNA fibrils using DNA origami and the A-motif. Visible light controls assembly and disassembly, offering a recyclable, non-modified approach for nanotechnology applications.
Area of Science:
- Biotechnology
- Nanotechnology
- Materials Science
Background:
- Hierarchical DNA nanostructures are programmable but lack dynamic control.
- Maintaining component integrity during dynamic assembly is a significant challenge.
Purpose of the Study:
- To develop a method for creating dynamic, hierarchical DNA nanostructures.
- To enable temporal control over DNA assembly and disassembly without chemical modification.
Main Methods:
- Utilized the DNA A-motif (protonated poly(adenine) sequences) to propagate DNA origami into fibrils.
- Employed a small molecule pH regulator activated by visible light to control hierarchical assembly.
- Developed a modular and waste-free strategy for assembly and disassembly.
Main Results:
- Successfully propagated DNA origami into one-dimensional, micron-length fibrils using the A-motif.
- Demonstrated visible light-activated, pH-controlled hierarchical assembly into dissipative fibrils.
- Showcased a recyclable system that does not require DNA modification.
Conclusions:
- The A-motif coupled with pH regulation provides a facile route to dynamic DNA assemblies.
- This approach enables the transient construction of diverse DNA nanostructures with temporal control.
- The system has broad applications in dynamic and non-equilibrium nanotechnology.
Related Concept Videos
01:18Assembly of Cytoskeletal Filaments
20.8K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
20.8K
01:39Mechanism of Filopodia Formation
2.4K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.4K
01:35Disassembly of Intermediate Filaments
2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K
01:14Generation of Straight or Branched Actin Filaments
2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K
01:59Lagging Strand Synthesis
52.6K
During replication, the complementary strands in double-stranded DNA are synthesized at different rates. Replication first begins on the leading strand. Replication starts later, occurs more slowly, and proceeds discontinuously on the lagging strand.
There are several major differences between synthesis of the leading strand and synthesis of the lagging strand. 1) Leading strand synthesis happens in the direction of replication fork opening, whereas lagging strand synthesis happens in the...
There are several major differences between synthesis of the leading strand and synthesis of the lagging strand. 1) Leading strand synthesis happens in the direction of replication fork opening, whereas lagging strand synthesis happens in the...
52.6K
00:57Formation of Intermediate Filaments
3.1K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.1K