Hierarchical Assembly of DNA Filaments with Designer Elastic Properties
Source abstract
Abstract
The elastic features of protein filaments are encoded in their component units and in the way they are connected, thus defining a biunivocal relationship between the monomer and the result of its self-assembly. Using DNA origami approaches, we constructed a reconfigurable module, composed of two quasi-independent domains and four possible interfaces, capable of facial and lateral growing through specific recognition patterns. Whereas the flexibility of the intra-domains region can be regulated by switchable DNA motifs, the inter-domain interfaces feature mutually and self-complementary shapes, whose pairwise association leads to filaments of programmable periodicity and variable persistence length. Thus, we show here that the assembly pathway leading to oligomeric chains can be finely tuned and fully controlled, enabling the emulation of protein-like filaments using a single construction principle. Our approach results in artificial materials with a large variety of ultrastructures and bending strengths comparable, or even superior, to their natural counterparts.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Bacteriophages and microbial interactions · Modular Robots and Swarm Intelligence
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Centre for Medical Biotechnology (ZMB) and Centre for Nano Integration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Universitätstraße 2, 45117 Essen, Germany
Department of Structural Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Straße 11, 44227 Dortmund, Germany
Funding
Deutsche Forschungsgemeinschaft · Max-Planck-Gesellschaft
References (36)
Show source-provided references
1. 10.1073/pnas.07206559910.1073/pnas.072065599 ↗
2. 10.1038/nmat408910.1038/nmat4089 ↗
3. 10.1038/nmat447410.1038/nmat4474 ↗
4. 10.1016/j.sbi.2004.06.00610.1016/j.sbi.2004.06.006 ↗
5. 10.1016/0022-5193(82)90002-910.1016/0022-5193(82)90002-9 ↗
6. 10.1038/nature0140610.1038/nature01406 ↗
7. 10.1038/nature0458610.1038/nature04586 ↗
8. 10.1038/nature0659710.1038/nature06597 ↗
9. 10.1038/nature0801610.1038/nature08016 ↗
10. 10.1126/science.122726810.1126/science.1227268 ↗
11. 10.1038/nature1107510.1038/nature11075 ↗
12. 10.1038/nnano.2015.16210.1038/nnano.2015.162 ↗
13. 10.1038/nature1458610.1038/nature14586 ↗
14. 10.1126/science.aaa537210.1126/science.aaa5372 ↗
15. 10.1038/nchem.107010.1038/nchem.1070 ↗
16. 10.1002/cbic.20160003410.1002/cbic.201600034 ↗
17. 10.1038/nature0827410.1038/nature08274 ↗
18. Zhang, T.; Hartl, C.; Fischer, S.; Frank, K.; Nickels, P.; Heuer-Jungemann, A.; Nickel, B.; Liedl, T.3D DNA Origami Crystals.arXiv.1706.06965v1, 2017.10.1002/adma.201800273 ↗
19. 10.1073/pnas.030586010110.1073/pnas.0305860101 ↗
20. 10.1021/ja044319l10.1021/ja044319l ↗
21. 10.1021/nn401362p10.1021/nn401362p ↗
22. 10.1088/0957-4484/22/27/27530110.1088/0957-4484/22/27/275301 ↗
23. 10.1038/nnano.2010.10710.1038/nnano.2010.107 ↗
24. 10.1039/C4NR07153K10.1039/C4NR07153K ↗
25. 10.1021/nn405408g10.1021/nn405408g ↗
26. 10.1111/febs.1333610.1111/febs.13336 ↗
27. 10.1146/annurev.biophys.29.1.10510.1146/annurev.biophys.29.1.105 ↗
28. 10.1016/j.str.2014.10.01310.1016/j.str.2014.10.013 ↗
29. 10.1093/nar/gkr117310.1093/nar/gkr1173 ↗
30. 10.1186/1751-0473-9-1610.1186/1751-0473-9-16 ↗
31. 10.1006/jmbi.1996.068710.1006/jmbi.1996.0687 ↗
32. 10.1002/anie.20140599110.1002/anie.201405991 ↗
33. 10.1038/nature1198710.1038/nature11987 ↗
34. 10.1038/ncomms1447210.1038/ncomms14472 ↗
35. 10.1016/j.jsb.2006.05.00910.1016/j.jsb.2006.05.009 ↗
36. 10.3791/5544810.3791/55448 ↗