Strand Displacement in Coiled‐Coil Structures: Controlled Induction and Reversal of Proximity

Gröger, Katharina; Gavins, Georgina; Seitz, Oliver

doi:10.1002/anie.201705339

Cited by 30 publications

(37 citation statements)

References 61 publications

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“…energy transfer dyes, nanoparticles, drugs) in close proximity, or with a higher density, than modifying origami staple strands alone. Several reports have showed that coil assembly can be controlled with light using azobenzenes, 30 or that coils can be displaced similar to DNA 8,9 by introducing an unpaired partial heptad "toehold"; 31 both of these mechanisms can in principle now be used to dynamically control DNA structure selfassembly. Finally, we note that coiled-coil DNA conjugates will enable integration of recombinant proteins through genetic fusion of one of the two peptide partners, and may enhance the stability of hybrid nanomaterials by not requiring supraphysiological counterion concentrations.…”

Section: Discussionmentioning

confidence: 99%

Hierarchical Assembly of DNA Origami Nanostructures Using Coiled-coil Peptides

Buchberger¹,

Simmons²,

Fahmi³

et al. 2019

Preprint

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DNA and peptides are two of the most commonly used biomolecules for building self-assembling materials, but few examples exist of hybrid nanostructures that contain both components. Here we report the modification of two peptides that comprise a coiled-coil heterodimer pair with orthogonal DNA handles in order to link DNA origami nanostructures bearing complementary strands into micrometer long one-dimensional arrays. We probed the effect of number of coils on self-assembly and demonstrated the formation of self-assembled structures through multiple routes, to form dimers and trimers, an alternating copolymer of two different origami bundles, and stepwise assembly of purified structures with coiled-coil conjugates. Our results demonstrate the successful merging of two distinct self-assembly modes to create hybrid bionanomaterials expected to have a range of potential applications in the future.

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Section: Discussionmentioning

confidence: 99%

Hierarchical Assembly of DNA Origami Nanostructures Using Coiled-coil Peptides

Buchberger¹,

Simmons²,

Fahmi³

et al. 2019

Preprint

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“…1 Eklund et al started with the E 3 /K 3 coiled coil pair of 21 amino acid (aa) peptides, where each E unit is a negatively charged 7 aa "heptad repeat" and each K unit is a positively charged 7 aa "heptad repeat" peptide. [26][27][28] Keeping the length of the negatively charged peptide constant, Eklund et al explored the effect of decreasing the length of the K peptide on coiled coil stability. They chose to work with K peptides of 18 or 19 aa, which interact with the E peptide with dissociation constants of 1.7 μM and 81 nM, respectively.…”

Section: Protein-based Paint Methodsmentioning

confidence: 99%

PAINT using proteins: A new brush for super‐resolution artists

Mochrie

Horrocks

et al. 2020

Protein Science

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PAINT (points accumulation for imaging in nanoscale topography) refers to methods that achieve the sparse temporal labeling required for super-resolution imaging by using transient interactions between a biomolecule of interest and a fluorophore. There have been a variety of different implementations of this method since it was first described in 2006. Recent papers illustrate how transient peptide-protein interactions, rather than small molecule binding or DNA oligonucleotide duplex formation, can be employed to perform PAINT-based single molecule localization microscopy (SMLM). We discuss the different approaches to PAINT using peptide and protein interactions, and their applications in vitro and in vivo. We highlight the important parameters to consider when selecting suitable peptide-protein interaction pairs for such studies. We also note the opportunities for protein scientists to apply their expertise in guiding the choice of peptide and protein pairs that are used. Finally, we discuss the potential for expanding super-resolution imaging methods based on transient peptide-protein interactions, including the development of simultaneous multicolor imaging of multiple proteins and the study of very high and very low abundance proteins in live cells.

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“…Hitherto, CC assemblies responsive to pH, metal ions, light, redox conditions, hydrophobic ligands or phosphorylation have been successfully designed. Additionally, CC strand displacement using peptides with different affinities to guide the exchange of CC assemblies has recently been presented . Metal ions are particularly suitable for controlling conformational changes due to their ubiquitous role in various biological systems .…”

Section: Methodsmentioning

confidence: 99%

SwitCCh: Metal‐Site Design for Controlling the Assembly of a Coiled‐Coil Homodimer

2018

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Conformational change of proteins in response to chemical or physical signals is the underlying principle of many regulatory and transport mechanisms in biological systems. The ability to design proteins the conformational state of which can be precisely and reversibly controlled would facilitate the development of molecular machines tailored for specific applications. Here we explore metal‐binding site design to engineer a peptide‐based conformational switch called SwitCCh that assembles into a homodimeric coiled‐coil in response to the addition of ZnII ions or low pH. Addition of ZnII promoted formation of a parallel homodimer with an increase in thermal stability by more than 30 °C. The peptide could be reversibly cycled between the coiled‐coil and random conformation. Furthermore, the SwitCCh peptide was orthogonal to the previously developed coiled‐coil dimer set, indicating it could be used for regulated self‐assembly of coiled‐coil based nanostructures and materials.

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Strand Displacement in Coiled‐Coil Structures: Controlled Induction and Reversal of Proximity

Cited by 30 publications

References 61 publications

Hierarchical Assembly of DNA Origami Nanostructures Using Coiled-coil Peptides

Hierarchical Assembly of DNA Origami Nanostructures Using Coiled-coil Peptides

PAINT using proteins: A new brush for super‐resolution artists

SwitCCh: Metal‐Site Design for Controlling the Assembly of a Coiled‐Coil Homodimer

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