Genetically Engineered Supercharged Polypeptide Fluids: Fast and Persistent Self‐Ordering Induced by Touch

Zhang, Lei; Ma, Chao; Sun, Jing; Shao, Baiqi; Portale, Giuseppe; Chen, Dong; Li, Kai; Herrmann, Andreas

doi:10.1002/anie.201803169

Cited by 43 publications

(24 citation statements)

References 34 publications

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“…The charged AAs are sites for additional chemical modifications, allowing for the creation of a virtually unlimited number of variations of these recombinant biopolymers. A consequence of this precise control over the amino acid composition along the unfolded polypeptide backbone is the possibility to introduce a multitude of desired properties …”

Section: Engineering Unstructured Supercharged Polypeptidesmentioning

confidence: 99%

“…Recently, we established a novel family of highly ionic repetitive polypeptides, termed supercharged unstructured polypeptides (SUPs) with NCD values higher than that reported for ELPs. This was achieved by introducing charged AAs into the pentapeptide VPGXG (Table ) wherein X represents the position of the charged AA . With this motif as starting point, SUPs were programmed with half of the charges employing (GVGVPGVGXP) n as repeat unit.…”

Section: Engineering Unstructured Supercharged Polypeptidesmentioning

confidence: 99%

“…Supercharging proteins and polypeptides thus provides materials with exciting properties such as hyper‐temperature resistance and the ability of overcoming biological barriers in vivo . Moreover, these highly charged structures allow the assembly of bioliquids, organelle‐like condensed matter architectures, artificial biological nanocontainers, and interfacial coatings among many others.…”

Section: Introductionmentioning

confidence: 99%

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Supercharged Proteins and Polypeptides

Malessa

Boersma

et al. 2020

Advanced Materials

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Electrostatic interactions play a vital role in nature. Biomacromolecules such as proteins are orchestrated by electrostatics, among other intermolecular forces, to assemble and organize biochemistry. Natural proteins with a high net charge exist in a folded state or are unstructured and can be an inspiration for scientists to artificially supercharge other protein entities. Recent findings show that supercharging proteins allows for control of their properties such as temperature resistance and catalytic activity. One elegant method to transfer the favorable properties of supercharged proteins to other proteins is the fabrication of fusions. Genetically engineered, supercharged unstructured polypeptides (SUPs) are just one promising fusion tool. SUPs can also be complexed with artificial entities to yield thermotropic and lyotropic liquid crystals and liquids. These architectures represent novel bulk materials that are sensitive to external stimuli. Interestingly, SUPs undergo fluid–fluid phase separation to form coacervates. These coacervates can even be directly generated in living cells or can be combined with dissipative fiber assemblies that induce life‐like features. Supercharged proteins and SUPs are developed into exciting classes of materials. Their synthesis, structures, and properties are summarized. Moreover, potential applications are highlighted and challenges are discussed.

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Section: Engineering Unstructured Supercharged Polypeptidesmentioning

confidence: 99%

Section: Engineering Unstructured Supercharged Polypeptidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Supercharged Proteins and Polypeptides

Malessa

Boersma

et al. 2020

Advanced Materials

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“…When the forces were unloaded, the fibers returned to their original conformation, and the resistance returned to its original value. The outstanding durability makes the BSA fiber a promising candidate for mechanical‐responsive applications …”

Section: Figurementioning

confidence: 99%

Mechanically Strong Globular‐Protein‐Based Fibers Obtained Using a Microfluidic Spinning Technique

Yang

Wang

et al. 2020

Angew Chem Int Ed

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Proteins used for the formation of light weight and mechanically strong biological fibers are typically composed of folded rigid and unfolded flexible units. In contrast to fibrous proteins, globular proteins are generally not regarded as a good candidate for fiber production due to their intrinsic structural defects. Thus, it is challenging to develop an efficient strategy for the construction of mechanically strong fibers using spherical proteins. Herein, we demonstrate the production of robust protein fibers from bovine serum albumin (BSA) using a microfluidic technique. Remarkably, the toughness of the fibers was up to 143 MJ m−3, and after post‐stretching treatment, their breaking strength increased to almost 300 MPa due to the induced long‐range ordered structure in the fibers. The performance is comparable to or even higher than that of many recombinant spider silks or regenerated silkworm fibers. Thus, this work opens a new way for making biological fibers with high performance.

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“…In addition, the mechanical properties of SUP‐surfactant fluids can be controlled by varying the chain length of the surfactant and molecular weight of SUPs. More interestingly, SUP fluids with fast self‐ordering behavior triggered by external shear forces were also developed by electrostatic complexation of SUPs and cationic surfactants containing azobenzene unit (Azo) . Those protein fluids exhibited sensitive isotropic–nematic (I–N) transition behavior which can be induced by different external forces including water flow and pressing with a fingertip.…”

Section: Protein‐based Adhesivesmentioning

confidence: 99%

Fabrication and Mechanical Properties of Engineered Protein‐Based Adhesives and Fibers

Sun

et al. 2019

Advanced Materials

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124

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Protein-based structural biomaterials are of great interest for various applications because the sequence flexibility within the proteins may result in their improved mechanical and structural integrity and tunability. As the two representative examples, protein-based adhesives and fibers have attracted tremendous attention. The typical protein adhesives, which are secreted by mussels, sandcastle worms, barnacles, and caddisfly larvae, exhibit robust underwater adhesion performance. In order to mimic the adhesion performance of these marine organisms, two main biological adhesives are presented, including genetically engineered protein-based adhesives and biomimetic chemically synthetized adhesives. Moreover, various protein-based fibers inspired by spider and silkworm proteins, collagen, elastin, and resilin are studied extensively. The achievements in synthesis and fabrication of structural biomaterials by DNA recombinant technology and chemical regeneration certainly will accelerate the explorations and applications of protein-based adhesives and fibers in wound healing, tissue regeneration, drug delivery, biosensors, and other high-tech applications. However, the mechanical properties of the biological structural materials still do not match those of natural systems. More efforts need to be devoted to the study of the interplay of the protein structure, cohesion and adhesion effects, fiber processing, and mechanical performance.

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Genetically Engineered Supercharged Polypeptide Fluids: Fast and Persistent Self‐Ordering Induced by Touch

Cited by 43 publications

References 34 publications

Supercharged Proteins and Polypeptides

Supercharged Proteins and Polypeptides

Mechanically Strong Globular‐Protein‐Based Fibers Obtained Using a Microfluidic Spinning Technique

Fabrication and Mechanical Properties of Engineered Protein‐Based Adhesives and Fibers

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