DNA-Mediated Assembly of Protein Heterodimers on Membrane Surfaces

Coyle, Michael P.; Xu, Qian; Chiang, Samantha; Francis, Matthew B.; Groves, Jay T.

doi:10.1021/ja3101215

Cited by 28 publications

(33 citation statements)

References 61 publications

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“…In contrast, oligonucleotide base-pairing interactions are well understood, form with high fidelity, and have been widely used as a means for assembling diverse supramolecular shapes that can act as scaffolds for organizing the assembly of external molecules, including proteins or protein-based virus capsids (35)(36)(37)(38)(39)(40). By replacing the formation of protein-protein interactions with oligonucleotide hybridization, we have shown that crystalline superlattices can be assembled from a single protein, multiple proteins, or a combination of proteins and AuNPs.…”

Section: Discussionmentioning

confidence: 99%

DNA-mediated engineering of multicomponent enzyme crystals

Brodin

Auyeung

Mirkin

2015

Proc. Natl. Acad. Sci. U.S.A.

131

138

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The ability to predictably control the coassembly of multiple nanoscale building blocks, especially those with disparate chemical and physical properties such as biomolecules and inorganic nanoparticles, has far-reaching implications in catalysis, sensing, and photonics, but a generalizable strategy for engineering specific contacts between these particles is an outstanding challenge. This is especially true in the case of proteins, where the types of possible interparticle interactions are numerous, diverse, and complex. Herein, we explore the concept of trading protein-protein interactions for DNA-DNA interactions to direct the assembly of two nucleic-acid-functionalized proteins with distinct surface chemistries into six unique lattices composed of catalytically active proteins, or of a combination of proteins and DNA-modified gold nanoparticles. The programmable nature of DNA-DNA interactions used in this strategy allows us to control the lattice symmetries and unit cell constants, as well as the compositions and habit, of the resulting crystals. This study provides a potentially generalizable strategy for constructing a unique class of materials that take advantage of the diverse morphologies, surface chemistries, and functionalities of proteins for assembling functional crystalline materials.nanoscience | biomaterials | self-assembly | superlattice | DNA-programmable assembly D NA-mediated assembly strategies (1-3) that take advantage of rigid building blocks, functionalized with oriented oligonucleotides to create entities with well-defined "valencies," have emerged as powerful new ways for programming the formation of crystalline materials (4, 5). With such methods, one can make architectures with well-defined lattice parameters (6-12), symmetries (4,8,10,12), and compositions (10, 12, 13), but to date they have been confined primarily to the use of hard inorganic nanoparticles (NPs) or highly branched pure nucleic-acid materials (2, 14, 15). In contrast, Nature's most powerful and versatile nanostructured building blocks are proteins and are used to effect the vast majority of processes in living systems (16). Unlike most inorganic NP systems, proteins can be made in pure and perfectly monodisperse form, making them ideal synthons for supramolecular assemblies. However, the ability to engineer lattices composed of multiple proteins, or of proteins and inorganic nanomaterials, has been limited, and the choice of protein building blocks is often restricted by structural constraints, which limits the catalytic functionalities that can be incorporated into these structures. Currently, the primary methods for making protein lattices have relied on the use of natural protein-protein interactions (17), interactions between proteins and ligands on the surfaces of inorganic NPs (17, 18), metal coordination chemistry (19), small molecule ligand-protein interactions (20-23), genetically fusing protein complexes with specific symmetries (24, 25), or DNA-mediated assembly of viruses (26,27). Here, we introduce a new...

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Section: Discussionmentioning

confidence: 99%

DNA-mediated engineering of multicomponent enzyme crystals

Brodin

Auyeung

Mirkin

2015

Proc. Natl. Acad. Sci. U.S.A.

131

138

View full text Add to dashboard Cite

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“…Despite notable recent achievements (32,33), the de novo design of protein-protein interactions, especially to form supramolecular structures beyond dimeric complexes, remains difficult due to a lack of universal interaction motifs (34). In contrast, oligonucleotide base-pairing interactions are well understood, form with high fidelity, and have been widely used as a means for assembling diverse supramolecular shapes that can act as scaffolds for organizing the assembly of external molecules, including proteins or protein-based virus capsids (35)(36)(37)(38)(39)(40). By replacing the formation of protein-protein interactions with oligonucleotide hybridization, we have shown that crystalline superlattices can be assembled from a single protein, multiple proteins, or a combination of proteins and AuNPs.…”

Section: Discussionmentioning

confidence: 99%

DNA-Mediated Engineering of Multicomponent Enzyme Crystals*

Brodin¹,

Auyeung²,

Mirkina³

2020

Spherical Nucleic Acids

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“…They then constructed a paracrine signaling network in these isolated artificial 3D microtissues. In addition to patterning cells, another study reported by Coyle et al [133] has shown that a DNAbased strategy can also be used to mediate the assembly of proteins into defined heterodimers or higher-order oligomers on supported membranes, which can then be used to direct the molecular composition of cell membrane receptor clusters. Moreover, instead of using simple ssDNA strands, Langecker et al [134] used scaffolded DNA origami to create lipid membrane channels composed of a stem that penetrated and spanned a lipid membrane, as well as a barrel-shaped cap that adhered to the membrane ( Figure 6E).…”

Section: Surface Engineering Of Live Cell With Dna Nanostructuresmentioning

confidence: 99%

Bio-surface engineering with DNA scaffolds for theranostic applications

et al. 2018

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Biosensor design is important to bioanalysis yet challenged by the restricted target accessibility at the biomolecule-surface (bio-surface). The last two decades have witnessed the appearance of various "art-like" DNA nanostructures in one, two, or three dimensions, and DNA nanostructures have attracted tremendous attention for applications in diagnosis and therapy due to their unique properties (e.g., mechanical flexibility, programmable control over their shape and size, easy and high-yield preparation, precise spatial addressability and biocompatibility). DNA nanotechnology is capable of providing an effective approach to control the surface functionality, thereby increasing the molecular recognition ability at the biosurface. Herein, we present a critical review of recent progress in the development of DNA nanostructures in one, two and three dimensions and highlight their biological applications including diagnostics and therapeutics. We hope that this review provides a guideline for bio-surface engineering with DNA nanostructures.

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DNA-Mediated Assembly of Protein Heterodimers on Membrane Surfaces

Cited by 28 publications

References 61 publications

DNA-mediated engineering of multicomponent enzyme crystals

DNA-mediated engineering of multicomponent enzyme crystals

DNA-Mediated Engineering of Multicomponent Enzyme Crystals*

Bio-surface engineering with DNA scaffolds for theranostic applications

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