Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Mohammadi, Pezhman; Zemke, Fabian; Wagermaier, Wolfgang

doi:10.3390/ma14154239

Cited by 10 publications

(7 citation statements)

References 48 publications

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“…Previously, Mohammadi et al. showed that similar silk-like proteins can self-assemble at the water–air interface of a droplet in a manner that is both time- and RH-dependent . Furthermore, they noticed a significant difference in the β-sheet content between 40 and 80% RH, an observation consistent with our findings that the most dramatic change happens in the range of 45–65% RH.…”

Section: Resultssupporting

confidence: 91%

“…showed that similar silk-like proteins can self-assemble at the water–air interface of a droplet in a manner that is both time- and RH-dependent . Furthermore, they noticed a significant difference in the β-sheet content between 40 and 80% RH, an observation consistent with our findings that the most dramatic change happens in the range of 45–65% RH. The effect of the protein concentration on CA indicates that a moderate amount of protein is better provided that the film contains enough protein for full surface coverage.…”

Section: Resultssupporting

confidence: 90%

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Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method

et al. 2023

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Molecular engineering of protein structures offers a uniquely versatile route for novel functionalities in materials. Here, we describe a method to form highly hydrophobic thin films using genetically engineered spider silk proteins. We used structurally engineered protein variants containing ADF3 and AQ12 spider silk sequences. Wetting properties were studied using static and dynamic contact angle measurements. Solution conditions and the surrounding humidity during film preparation were key parameters to obtain high hydrophobicity, as shown by contact angles in excess of 120°. Although the surface layer was highly hydrophobic, its structure was disrupted by the added water droplets. Crystal-like structures were found at the spots where water droplets had been placed. To understand the mechanism of film formation, different variants of the proteins, the topography of the films, and secondary structures of the protein components were studied. The high contact angle in the films demonstrates that the conformations that silk proteins take in the protein layer very efficiently expose their hydrophobic segments. This work reveals a highly amphiphilic nature of silk proteins and contributes to an understanding of their assembly mechanisms. It will also help in designing diverse technical uses for recombinant silk.

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Section: Resultssupporting

confidence: 91%

Section: Resultssupporting

confidence: 90%

Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method

et al. 2023

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“…Measurements were performed with an energy exposure of 15 keV (0.82656 Å) using a silicon 111 monochromator and a beam size of 100 μm. Data were recorded using an Eiger X 9M detector with a pixel size of 75 μm × 75 μm, as reported previously ( 56 , 57 ). The measurements were carried out under ambient conditions at 50% RH.…”

Section: Methodsmentioning

confidence: 99%

The complex structure of Fomes fomentarius represents an architectural design for high-performance ultralightweight materials

et al. 2023

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High strength, hardness, and fracture toughness are mechanical properties that are not commonly associated with the fleshy body of a fungus. Here, we show with detailed structural, chemical, and mechanical characterization that Fomes fomentarius is an exception, and its architectural design is a source of inspiration for an emerging class of ultralightweight high-performance materials. Our findings reveal that F . fomentarius is a functionally graded material with three distinct layers that undergo multiscale hierarchical self-assembly. Mycelium is the primary component in all layers. However, in each layer, mycelium exhibits a very distinct microstructure with unique preferential orientation, aspect ratio, density, and branch length. We also show that an extracellular matrix acts as a reinforcing adhesive that differs in each layer in terms of quantity, polymeric content, and interconnectivity. These findings demonstrate how the synergistic interplay of the aforementioned features results in distinct mechanical properties for each layer.

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“…The foams were fabricated through a very simple and scalable process, which involved gently introducing air bubbles into the 4RepCT solution. The process was continued until the stable foam was formed by the self-assembly of 4RepCT proteins at the air–water interface …”

Section: Bioengineering Of Protein-based Materialsmentioning

confidence: 99%

Protein-Based Biological Materials: Molecular Design and Artificial Production

Miserez

Mohammadi

2023

Chem. Rev.

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Polymeric materials produced from fossil fuels have been intimately linked to the development of industrial activities in the 20th century and, consequently, to the transformation of our way of living. While this has brought many benefits, the fabrication and disposal of these materials is bringing enormous sustainable challenges. Thus, materials that are produced in a more sustainable fashion and whose degradation products are harmless to the environment are urgently needed. Natural biopolymerswhich can compete with and sometimes surpass the performance of synthetic polymersprovide a great source of inspiration. They are made of natural chemicals, under benign environmental conditions, and their degradation products are harmless. Before these materials can be synthetically replicated, it is essential to elucidate their chemical design and biofabrication. For protein-based materials, this means obtaining the complete sequences of the proteinaceous building blocks, a task that historically took decades of research. Thus, we start this review with a historical perspective on early efforts to obtain the primary sequences of load-bearing proteins, followed by the latest developments in sequencing and proteomic technologies that have greatly accelerated sequencing of extracellular proteins. Next, four main classes of protein materials are presented, namely fibrous materials, bioelastomers exhibiting high reversible deformability, hard bulk materials, and biological adhesives. In each class, we focus on the design at the primary and secondary structure levels and discuss their interplays with the mechanical response. We finally discuss earlier and the latest research to artificially produce protein-based materials using biotechnology and synthetic biology, including current developments by start-up companies to scale-up the production of proteinaceous materials in an economically viable manner.

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Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Cited by 10 publications

References 48 publications

Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method

Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method

The complex structure of Fomes fomentarius represents an architectural design for high-performance ultralightweight materials

Protein-Based Biological Materials: Molecular Design and Artificial Production

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