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>3.3.co;2-4

Cited by 36 publications

(51 citation statements)

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“…For example, the molecular recognition between carbohydrate and lectin is adopted by pathogens for their adhesion to host tissues. In laboratories, the specific binding between carbohydrates and lectins was well characterized by X-ray crystallography 56 , ITC 57 , SPR 58 In the examples of using ditopic molecules just mentioned, the two saccharide units were linked via covalent bonds, thus the formation mechanism of the 1D or 3D array was similar to that of condensation polymerization, in which strictly controlled 1:1 ratio of protein binding sites and sugar motifs was required 60 . This criterion limited the obtained morphologies and the assembly speed as well.…”

Section: Protein Self-assembly Driven By Molecular Recognitionmentioning

confidence: 99%

Precise protein assembly of array structures

Yang

Chen

et al. 2016

Chem. Commun.

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The assembly of proteins into various nano-objects with regular and periodic microstructures, i.e. protein arrays, is a fast-growing field in materials science. Due to the structural complexity of proteins, reports in this field are still quite limited. In this review, we summarize the recent developments in protein array construction by different driving forces, including electrostatic interactions, metal-ligand interactions, molecular recognition and protein-protein interactions. In line with our particular interest, assemblies driven by molecular recognition are particularly explored. Finally, functionalities of the obtained protein arrays are briefly discussed.

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Section: Protein Self-assembly Driven By Molecular Recognitionmentioning

confidence: 99%

Precise protein assembly of array structures

Yang

Chen

et al. 2016

Chem. Commun.

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“…Protein crystals present highly ordered 3D arrangements of protein molecules with high porosity (0.5–0.8) and a wide range of pore sizes (ca. 1–10 nm) 14–16. The size and morphology of pores in protein crystals depend on the surface characteristics of proteins and the crystallization conditions.…”

Section: Characteristics Of the Copt‐nps Prepared In The Hewl Crystalmentioning

confidence: 99%

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

Abe

Tsujimoto

Yoneda³

et al. 2012

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“…Previous efforts in designed protein self-assembly have had limited success: they have generally required building blocks with high preexisting symmetry, allowed little or no external control over self-assembly, and yielded static protein architectures that did not display long-range order beyond a few hundred nanometers 14-18 .…”

Section: Introductionmentioning

confidence: 99%

Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays

et al. 2012

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Proteins represent the most sophisticated building blocks available to an organism or the laboratory chemist. Yet, in contrast to nearly all other types of molecular building blocks, the designed self-assembly of proteins has been largely inaccessible owing to the chemical and structural heterogeneity of protein surfaces. To circumvent the challenge of programming extensive non-covalent interactions for controlling protein self-assembly, we had previously exploited the directionality and strength of metal coordination interactions to guide the formation of closed, homoligomeric protein assemblies. Here, we extend this strategy to the generation of periodic protein arrays. We show that a monomeric protein with properly oriented coordination motifs on its surface can arrange upon metal binding into one-dimensional nanotubes, and two-or three-dimensional crystalline arrays whose dimensions collectively span nearly the entire nano- and micrometer length scale. The assembly of these arrays is predictably tuned by external stimuli, such as metal concentration and pH.

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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 36 publications

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Precise protein assembly of array structures

Precise protein assembly of array structures

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays

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