A Superhydrophobic Surface Templated by Protein Self‐Assembly and Emerging Application toward Protein Crystallization

Gao, Aiting; Wu, Qian; Wang, Dehui; Ha, Yuan; Chen, Zhijun; Yang, Peng

doi:10.1002/adma.201504769

Cited by 143 publications

(100 citation statements)

References 72 publications

(61 reference statements)

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“…While TCEP reduced GO to rGO efficiently, it would also simultaneously reduce the disulfide bond of lysozyme to trigger fast amyloid‐like protein aggregation. [ 25,26 ] Consequently, after incubating the mixture solution of lysozyme, GO, and TCEP at a given temperature for a given time, a homogeneous PTL/rGO hybrid coating with a highly integrated sp 2 carbon network of rGO could be prepared by casting the mixture into a mold and evaporating away the water ( Figure a).…”

Section: Resultsmentioning

confidence: 99%

“…[ 21–23 ] A typical amyloid protein lysozyme could undergo a unique fast conformational change (called a phase transition) in aqueous solution when mixed with tris(2‐carboxyethyl)phosphine (TCEP). [ 24,25 ] During this phase transition process, the α‐helix of native lysozyme unfolds and assembles into a β‐sheet structure after the disulfide bonds of the lysozyme chain are broken by TCEP, [ 26 ] resulting in the formation of amyloid‐like assembled oligomers (called phase‐transited lysozyme, PTL) that exhibit stable adhesion to virtually arbitrary substrate surfaces by constructing multiscale polyvalent molecular and structural interactions with the underlying substrate. [ 27,28 ] In addition to the capability of TCEP toward the disulfide bond reduction of a protein, in the present work, we discover that TCEP is also a highly effective reducing agent for GO.…”

Section: Introductionmentioning

confidence: 99%

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Controlling Long‐Distance Photoactuation with Protein Additives

Zhao

Miao

et al. 2020

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Long-distance wireless actuation indicates precise remote control over materials, sensors, and devices that are widely utilized in biomedical, defence, disaster relief, deep ocean, and outer space applications to replace human work. Unlike radio frequency (RF) control, which has low tolerance toward electromagnetic interference (EMI), light control represents a promising method to overcome EMI. Nonetheless, long-distance lightcontrolled wireless actuation able to compete with RF control has not been achieved until now due to the lack of highly light-sensitive actuator designs. Here, it is demonstrate that amyloid-like protein aggregates can organize photomodule single-layer reduced graphene oxide (rGO) into a well-defined multilayer stack to display long-distance photoactuation. The amyloid-like proteinaceous component docks the rGO layers together to form a hybrid film, which can reliably adhere onto various material surfaces with robust interfacial adhesion. The sensitive photothermal effect and a fast bending in 1 s to switch a circuit are achieved after forming the film on a plastic substrate and irradiating the bilayer film with a blue laser from 100 m away. A photoactuation distance of 50 km can be further extrapolated based on a commercial high-power laser. This study reveals the great potential of amyloid-like aggregates in remote light control of robots and devices.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Controlling Long‐Distance Photoactuation with Protein Additives

Zhao

Miao

et al. 2020

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“…In designing our new way, we use the fact that a superhydrophobic amyloid‐like biointerface was able to work as an excellent platform for protein crystallization . Conventionally, hanging‐drop vapor diffusion is a typical protein crystallization method, which needs a condition of supersaturation of a protein solution.…”

Section: Resultsmentioning

confidence: 99%

“…These parameters often make the whole process to be tedious, time‐consuming, and toxic (e.g., some harmful precipitants) to human. In contrast, the superhydrophobic biointerface offered relatively mild strategy for its great feasibility to concentrate solutes in the sessile droplet to offer biomolecular crystal growth . Moreover, the superhydrophobic biointerface is based on proteins with many function groups decorated, such as methyl, thiol, and amino groups as well as micro/nanostructures, which can offer abundant active nucleation sites to promote the growth of high‐quality protein crystals .…”

Section: Resultsmentioning

confidence: 99%

Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface

Gao

Tao

et al. 2018

Adv Materials Inter

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biohybrids. [6] With respect to the crystallization, a protein-based biopolymer substrate is typically utilized in nature to develop excellent biomineralization system. [7] Vice versa, the utilization of mineral substrates, [8] chemically modified mica, [9] gel, [10] silanized polystyrene wells, [11] lipid layers, [12] polymeric film surfaces [13] as well as porous media, [14] etc. have contributed a lot to protein crystallization. Some conjectures have been made from these studies, typically including concentration effect-induced change of supersaturation extent near a surface, [15] adsorption of solutes on a surface, [16] specific interaction between solutes and chemically modified surfaces, [17] the presence of surface microtopography, and spatial characteristics to guide nucleation and crystalline lattice. [18] However, despite immense progress, understanding the crystallization mechanism of proteins and peptides on solid surface remains elusive, and more fundamental clues to reveal this process should be discovered. In this regard, a superhydrophobic surface would be an ideal platform for the crystallization design, since such an interface exhibits great feasibility to concentrate solutes in the sessile droplet [19] and this simplified model induces efficient crystallization of salts, [20] colloidal assembly [21] as well as detection enhancement. [22] Such a platform actually has found a wide range of important applications in current medicine and biotechnology, [23] such as protein adsorption, [24a] drug release, [24b,c] cellular interaction, [24d] and so on. [24e]

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“…In this context, lysozyme and Fe 3 O 4 NPs exhibit a strong interaction that may be attributed to their electrostatic interactions. By incorporating carboxyl‐modified Fe 3 O 4 NPs into the reaction solution, we previously studied their ability to modulate seeded and unseeded HEWL fibrillisation kinetics as well as the morphology of the formed microcapsules. Here we show a clear inhibition of HEWL fibrillisation in the presence of carboxyl‐modified Fe 3 O 4 NPs in unseeded conditions, while under seeded conditions, the fibrillisation process takes place, thus allowing extensive decoration of the fibrillary microcapsules.…”

Section: Introductionmentioning

confidence: 99%

Self‐assembled Protein Fibril‐metal Oxide Nanocomposites

Levin

Mason

Knowles

et al. 2017

Israel Journal of Chemistry

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Protein aggregation is commonly associated with the onset and development of neurodegenerative disorders, including Alzheimer's, Parkinson's and other forms of pathological disorders. While this phenomenon has historically been studied in the context of its relevance to human health, over the past decade significant research effort has focused on utilizing amyloid‐like protein assemblies as building blocks for the development of functional biomaterials and a number of protein‐based functional materials have been demonstrated. Here we extend this concept by synthesizing hybrid organic/inorganic microcapsules containing metal‐based NPs and protein nanofibrils as a nanocomposite. To this effect, we exploit the propensity of lysozyme to self‐assemble into amyloid nanofibrils and their functionalization by carboxyl‐modified Fe3O4 NPs. We use a microfluidics‐based approach to control the micron scale moprhology of the newly formed nanocomposites. Our results illustrate the potential ofthis strategy as a platform for fabricating microcapsules from nanofibril‐inorganic NPs hybrid materials.

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A Superhydrophobic Surface Templated by Protein Self‐Assembly and Emerging Application toward Protein Crystallization

Cited by 143 publications

References 72 publications

Controlling Long‐Distance Photoactuation with Protein Additives

Controlling Long‐Distance Photoactuation with Protein Additives

Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface

Self‐assembled Protein Fibril‐metal Oxide Nanocomposites

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