Self-Assembly of a Tetrahedral Lectin into Predesigned Diamondlike Protein Crystals

Dotan, Nir; Arad, Dorit; Frolow, Felix; Freeman, Amihay

doi:10.1002/(sici)1521-3773(19990816)38:16<2363::aid-anie2363>3.0.co;2-d

Cited by 73 publications

(23 citation statements)

References 10 publications

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“…1d). By using different approaches, some success has been reported already with nucleic acids (10) and with a carbohydrate-binding protein designed to assemble into an ordered array (20). Well ordered molecular layers may have applications as biosensors or detectors (21).…”

Section: Resultscontrasting

confidence: 99%

Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments

Padilla

Colovos

Yeates

2001

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

440

450

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A general strategy is described for designing proteins that self assemble into large symmetrical nanomaterials, including molecular cages, filaments, layers, and porous materials. In this strategy, one molecule of protein A, which naturally forms a self-assembling oligomer, A n, is fused rigidly to one molecule of protein B, which forms another self-assembling oligomer, B m. The result is a fusion protein, A-B, which self assembles with other identical copies of itself into a designed nanohedral particle or material, (A-B) p. The strategy is demonstrated through the design, production, and characterization of two fusion proteins: a 49-kDa protein designed to assemble into a cage approximately 15 nm across, and a 44-kDa protein designed to assemble into long filaments approximately 4 nm wide. The strategy opens a way to create a wide variety of potentially useful protein-based materials, some of which share similar features with natural biological assemblies.

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Section: Resultscontrasting

confidence: 99%

Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments

Padilla

Colovos

Yeates

2001

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

440

450

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“…Great effort has been devoted to the fabrication of protein crystals via, for example, fusing proteins to introduce required symmetry 2,7,8 or introducing small molecules to interact and link proteins [12][13][14] . An example of the outstanding progress achieved in recent years in this area is the strategy of metal-directed protein self-assembly, where protein-protein interaction is controlled through the introduction of metal coordination 10,15 .…”

mentioning

confidence: 82%

Protein crystalline frameworks with controllable interpenetration directed by dual supramolecular interactions

et al. 2014

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Protein crystalline frameworks are attractive for biomimetic and nanotechnological studies because they could augment the useful functionalities of numerous proteins through dense packing and uniform orientation. However, their formation and precise structural control is challenging. Here we present novel protein crystalline frameworks with controllable interpenetration. The homotetrameric lectin concanavalin A is crosslinked by predetermined inducing ligands containing monosaccharide and rhodamine groups connected by an oligo(ethylene oxide) spacer. Two non-covalent interactions, that is, sugar-lectin binding and the dimerization of RhB, are responsible for the framework formation. The three-dimensional structure of the framework is fully characterized by X-ray crystallographic methods. For the first time, either interpenetrating or non-interpenetrating frameworks are obtained, and they are controlled by the spacer length of the inducing ligand. Further kinetics and mechanistic investigations reveal that, in the self-assembly process, the carbohydrate-protein binding occurs first, followed by RhB dimerization. This sequence favours rapid crystallization with a high yield when an excess amount of inducing ligand is used. In short, by using wellcontrolled dual non-covalent interactions, fast and versatile preparation of protein crystalline framework was achieved with high crystallization ratio of the proteins, which may shed light on protein crystallization in near future.

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“…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)(21)(22)(23), genetically fusing protein complexes with specific symmetries (24,25), or DNA-mediated assembly of viruses (26,27). Here, we introduce a new method for effecting protein crystallization by trading protein-protein interactions for complementary oligonucleotide-oligonucleotide interactions.…”

mentioning

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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Self-Assembly of a Tetrahedral Lectin into Predesigned Diamondlike Protein Crystals

Abstract: Binding sites analogous to those of sp(3) carbon are presented by concanavalin A. This lectin has now been cross-linked with a bismannopyranoside which contains the C(2) spacer required to form the computer-modeled diamondlike three-dimensional protein lattice shown in the picture.

Cited by 73 publications

References 10 publications

Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments

Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments

Protein crystalline frameworks with controllable interpenetration directed by dual supramolecular interactions

DNA-mediated engineering of multicomponent enzyme crystals

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