Construction of Protein Nanowires through Cucurbit[8]uril‐based Highly Specific Host–Guest Interactions: An Approach to the Assembly of Functional Proteins

Hou, Chunxi; Li, Jiaxi; Zhao, Linlu; Zhang, Wei; Luo, Quan; Dong, Zeyuan; Xu, Jing; Liu, Junqiu

doi:10.1002/anie.201300692

Cited by 148 publications

(97 citation statements)

References 31 publications

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“…to be considered. Recently the host-guest interaction based on cucurbit [8]uril (CB [8]) was employed by Liu and his coworkers 66 . Short oligopeptide chain Phe-Gly-Gly (FGG) was engineered to the surface of GST dimer on opposite directions.…”

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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“…[1] In nature, proteins self-assemble into different structures in nano-or micrometer scale with highly ordered patterns, [2] forexample, virus capsids, [3] actin filaments, [4] microtubules, [5] and bacteria S-layers [6] .T hese attractive structures have stimulated strong motivation for programming proteins into various nanoobjects, [7] including oligomers, [8a,b] zero-dimensional (0D) nanocages, [8b,c] 1D fibers, [9] nanotubes, [10] 2D nanosheets, [11] nanorings, [12] and 3D frameworks [13] . [1] In nature, proteins self-assemble into different structures in nano-or micrometer scale with highly ordered patterns, [2] forexample, virus capsids, [3] actin filaments, [4] microtubules, [5] and bacteria S-layers [6] .T hese attractive structures have stimulated strong motivation for programming proteins into various nanoobjects, [7] including oligomers, [8a,b] zero-dimensional (0D) nanocages, [8b,c] 1D fibers, [9] nanotubes, [10] 2D nanosheets, [11] nanorings, [12] and 3D frameworks [13] .…”

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confidence: 99%

Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands

et al. 2017

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In nature, proteins self-assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally proteins with different symmetries are selected. However, most of these approaches are engineering-intensive and highly dependent on the accuracy of the protein design. Herein, we report that a simple native protein LecA assembles into one-dimensional nanoribbons and nanowires, two-dimensional nanosheets, and three-dimensional layered structures controlled mainly by small-molecule assembly-inducing ligands RnG (n=1, 2, 3, 4, 5) with varying numbers of ethylene oxide repeating units. To understand the formation mechanism of the different morphologies controlled by the small-molecule structure, molecular simulations were performed from microscopic and mesoscopic view, which presented a clear relationship between the molecular structure of the ligands and the assembled patterns. These results introduce an easy strategy to control the assembly structure and dimension, which could shed light on controlled protein assembly.

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“…This unique combination of properties has enabled numerous applications in the life sciences, for example, for protein binding [5–6], stabilization [7], immobilisation [8], isolation [9], self-assembly [10–11], and regulation [12], or for drug solubilisation and delivery [13–15]. …”

Section: Introductionmentioning

confidence: 99%

Rational design of boron-dipyrromethene (BODIPY) reporter dyes for cucurbit[7]uril

Alnajjar¹,

Bartelmeß²,

Hein³

et al. 2018

Beilstein J. Org. Chem.

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We introduce herein boron-dipyrromethene (BODIPY) dyes as a new class of fluorophores for the design of reporter dyes for supramolecular host–guest complex formation with cucurbit[7]uril (CB7). The BODIPYs contain a protonatable aniline nitrogen in the meso-position of the BODIPY chromophore, which was functionalized with known binding motifs for CB7. The unprotonated dyes show low fluorescence due to photoinduced electron transfer (PET), whereas the protonated dyes are highly fluorescent. Encapsulation of the binding motif inside CB7 positions the aniline nitrogen at the carbonyl rim of CB7, which affects the pK a value, and leads to a host-induced protonation and thus to a fluorescence increase. The possibility to tune binding affinities and pK a values is demonstrated and it is shown that, in combination with the beneficial photophysical properties of BODIPYs, several new applications of host–dye reporter pairs can be implemented. This includes indicator displacement assays with favourable absorption and emission wavelengths in the visible spectral region, fluorescence correlation spectroscopy, and noncovalent surface functionalization with fluorophores.

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Construction of Protein Nanowires through Cucurbit[8]uril‐based Highly Specific Host–Guest Interactions: An Approach to the Assembly of Functional Proteins

Cited by 148 publications

References 31 publications

Precise protein assembly of array structures

Precise protein assembly of array structures

Highly Ordered Self‐Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly‐Inducing Ligands

Rational design of boron-dipyrromethene (BODIPY) reporter dyes for cucurbit[7]uril

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