DNA-Mediated Engineering of Multicomponent Enzyme Crystals*

Brodin, Jeffrey D.; Auyeung, Evelyn; Mirkina, Chad A.

doi:10.1201/9781003056690-16

Cited by 3 publications

(3 citation statements)

References 37 publications

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“…Apart from typical PPIs, DNA-DNA interactions, coiled coil interactions, and other interactions produced by supramolecular self-associating components have been developed to build self-assembling superstructures by protein-based building blocks [10]. For instance, Brodin et al [11] connected oligonucleotides to catalase to construct crystalline superlattices by DNA-DNA interactions. Recent work on protein assemblies have been reviewed elsewhere [9,10].…”

Section: Introductionmentioning

confidence: 99%

Protein cages as building blocks for superstructures

Sun

Lim

2021

Engineering Biology

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Proteins naturally self‐assemble to function. Protein cages result from the self‐assembly of multiple protein subunits that interact to form hollow symmetrical structures with functions that range from cargo storage to catalysis. Driven by self‐assembly, building elegant higher‐order superstructures with protein cages as building blocks has been an increasingly attractive field in recent years. It presents an engineering challenge not only at the molecular level but also at the supramolecular level. The higher‐order constructs are proposed to provide access to diverse functional materials. Focussing on design strategy as a perspective, current work on protein cage supramolecular self‐assembly are reviewed from three principles that are electrostatic, metal‐ligand coordination and inherent symmetry. The review also summarises possible applications of the superstructure architecture built using modified protein cages.

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Section: Introductionmentioning

confidence: 99%

Protein cages as building blocks for superstructures

Sun

Lim

2021

Engineering Biology

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“…First, the group demonstrated that, similar to nanoparticles, proteins can be assembled via DNA ligands into predictable lattice symmetries and lattice parameters. 2 Next, the lab took advantage of the chemical anisotropy of protein surfaces to achieve an anisotropic arrangement of DNA ligands on b-galactosidase and green fluorescent protein (GFP). The anisotropic arrangement of DNA ligands changed the crystal symmetry of b-galactosidase co-assembled with nanoparticles.…”

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confidence: 99%

How to Become a Protein Crystallographer in a Nanoscience Lab

Winegar

2020

Chem

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Peter H. Winegar obtained his BS in chemistry at Michigan Technological University in 2017 under the mentorship of Prof. Loredana Valenzano. Currently, he is a PhD candidate in chemistry at Northwestern University and is advised by Prof. Chad A. Mirkin. Peter's current research includes the directed crystallization and oligomerization of proteins using DNA interactions. He serves on the board of Northwestern's Phi Lambda Upsilon Chemistry Honor Society and participates in science outreach to elementary students through Northwestern's Science in the Classroom program.The answer is innumerable hours of mentorship. Honestly, the amount of time and effort contributed by scientists toward my training is striking. Advisors, student and postdoc mentors, staff scientists, and peers have taught me invaluable scientific skills, including lab techniques, communication skills, and project management. I never doubted that I would be fascinated by the research topic of any group that I joined, but I made a focused effort to choose a lab with a strong culture of mentorship. I was fortunate to find this type of lab in the group of Prof. Chad Mirkin at Northwestern University.

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“…Here, particle interactions driven by the DNA bond afford deliberate architectural control with tunable bond length and strength 13,[21][22][23][24] . Indeed, one of the attractive features of this approach is that design rules have been established that allow one to control crystal symmetry, lattice parameter, and habit, independent of particle composition but dependent on particle size and shape [25][26][27] . Using a slow cooling approach, high-quality 3D single crystals can be produced 28,29 .…”

mentioning

confidence: 99%

Nonequilibrium Anisotropic Colloidal Single-Crystal Growth with DNA*

Seo¹,

Girard²,

Cruz³

et al. 2020

Spherical Nucleic Acids

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Anisotropic colloidal crystals are materials with novel optical and electronic properties. However, experimental observations of colloidal single crystals have been limited to relatively isotropic habits. Here, we show DNA-mediated crystallization of two types of nanoparticles with different hydrodynamic radii that form highly anisotropic, hexagonal prism microcrystals with AB 2 crystallographic symmetry. The DNA directs the nanoparticles to assemble into a non-equilibrium crystal shape that is enclosed by the highest surface energy facets (AB 2 (1010) and AB 2 (0001)). Simulations and theoretical arguments show that this observation is a consequence of large energy barriers between different terminations of the AB 2 (1010) facet, which results in a significant deceleration of the (1010) facet growth rate. In addition to reporting a hexagonal colloidal crystal habit, this work introduces a potentially general plane multiplicity mechanism for growing non-equilibrium crystal shapes, an advance that will be useful for designing colloidal crystal habits with important applications in both optics and photocatalysis.

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DNA-Mediated Engineering of Multicomponent Enzyme Crystals*

Cited by 3 publications

References 37 publications

Protein cages as building blocks for superstructures

Protein cages as building blocks for superstructures

How to Become a Protein Crystallographer in a Nanoscience Lab

Nonequilibrium Anisotropic Colloidal Single-Crystal Growth with DNA*

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