Dragline, Egg Stalk and Byssus: A Comparison of Outstanding Protein Fibers and Their Potential for Developing New Materials

Lintz, Eileen S.; Scheibel, Thomas

doi:10.1002/adfm.201300589

Cited by 39 publications

(31 citation statements)

References 204 publications

(214 reference statements)

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“…Rather, the HRD peptides formed dense amyloid-like phases under appropriate conditions of concentration and pH without metal ions present (Figure 9). [2,41] Notably, recent X-ray diffraction studies of native distal byssal threads have identified the presence of amyloid-like cross β-sheet structure; [14] however, it is unclear from the present investigation whether HRDs would still form amyloid phases within the thread. [2,41] Notably, recent X-ray diffraction studies of native distal byssal threads have identified the presence of amyloid-like cross β-sheet structure; [14] however, it is unclear from the present investigation whether HRDs would still form amyloid phases within the thread.…”

Section: Role Of Hrds In Precol Assemblymentioning

confidence: 79%

“…Protein-based materials formed extracorporeally (i.e., outside the body) similar to the mussel byssus (e.g., insect and spider silks [2] ) face two major challenges for material processing and assembly. Protein-based materials formed extracorporeally (i.e., outside the body) similar to the mussel byssus (e.g., insect and spider silks [2] ) face two major challenges for material processing and assembly.…”

Section: Structure-function Relationshipsmentioning

confidence: 99%

“…[1,2] Mussels, for example, use a robust proteinaceous holdfast known as a byssus to withstand incessant loading forces from crashing waves ( Figure 1A,B). [1,2] Mussels, for example, use a robust proteinaceous holdfast known as a byssus to withstand incessant loading forces from crashing waves ( Figure 1A,B).…”

Section: Introductionmentioning

confidence: 99%

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pH‐Responsive Self‐Organization of Metal‐Binding Protein Motifs from Biomolecular Junctions in Mussel Byssus

Reinecke

Brezesinski

Harrington

2016

Adv Materials Inter

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Mussels rapidly fabricate tough and self-healing biopolymeric fibers called byssal threads that provide an excellent role model for bio-inspired design. The remarkable tensile properties arise from a collagenous protein family known as preCols, which self-assemble into a semicrystalline array in the distal thread core. Histidine-rich domains (HRDs) at the preCol ends are critical both for the self-healing capacity and for the thread assembly process due to their propensity for coordinating transition metal ions; however, very little is understood about the molecular relationship between HRD sequence, structure, and function. Here, a comprehensive spectroscopic investigation of two model peptides based on conserved repetitive motifs in the HRDs is performed to elucidate molecular level details of their role in thread assembly and function. It is observed that environmental factors relevant to the natural assembly process (e.g., concentration, pH, and metal content) trigger dramatic changes in HRD nanostructure and higher order assembly, leading to the formation of highly defined backbone conformation and metal binding geometry

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Section: Role Of Hrds In Precol Assemblymentioning

confidence: 79%

Section: Structure-function Relationshipsmentioning

confidence: 99%

See 1 more Smart Citation

pH‐Responsive Self‐Organization of Metal‐Binding Protein Motifs from Biomolecular Junctions in Mussel Byssus

Reinecke

Brezesinski

Harrington

2016

Adv Materials Inter

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“…We found that proteins with high amounts of glycine, tyrosine and serine formed the epicuticular structures. The composition of the amino acid mixture resembled that of known structural proteins such as fibroin, collagen or resilin [30 -32], which often combine stiffness and toughness [35]. Thus, it can be reasonably assumed that the durability of patterned epicuticle of T. bielanensis to withstand wear in soil habitats results from epicuticular protein structures.…”

Section: Discussionmentioning

confidence: 99%

The multi-layered protective cuticle of Collembola: a chemical analysis

Nickerl

Tsurkan

Hensel

et al. 2014

J. R. Soc. Interface.

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Collembola, also known as springtails, are soil-dwelling arthropods that typically respire through the cuticle. To avoid suffocating in wet conditions, Collembola have evolved a complex, hierarchically nanostructured, cuticle surface that repels water with remarkable efficiency. In order to gain a more profound understanding of the cuticle characteristics, the chemical composition and architecture of the cuticle of Tetrodontophora bielanensis was studied. A stepwise removal of the different cuticle layers enabled controlled access to each layer that could be analysed separately by chemical spectrometry methods and electron microscopy. We found a cuticle composition that consisted of three characteristic layers, namely, a chitinrich lamellar base structure overlaid by protein-rich nanostructures, and a lipid-rich envelope. The specific functions, composition and biological characteristics of each cuticle layer are discussed with respect to adaptations of Collembola to their soil habitat. It was found that the non-wetting characteristics base on a rather typical arthropod cuticle surface chemistry which confirms the decisive role of the cuticle topography.

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“…Biological fibers such as spider and cocoon silks are widely used as biological materials in diverse applications (Omenetto and Kaplan, 2010). They have been elucidated in great detail in terms of structure and mechanical properties (Lintz and Scheibel, 2013). However, a complete description of their hierarchical structure and assembly pathway is still underway (van Beek et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

The assembly of C. elegans lamins into macroscopic fibers

Zingerman-Koladko

Khayat

Harapin

et al. 2016

Journal of the Mechanical Behavior of Biomedical Materials

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Intermediate filament (IF) proteins are known mainly by their propensity to form viscoelastic filamentous networks within cells. In addition, IF-proteins are essential parts of various biological materials, such as horn and hagfish slime threads, which exhibit a range of mechanical properties from hard to elastic. These properties and their self-assembly nature made IF-proteins attractive building blocks for biomimetic and biological materials in diverse applications. Here we show that a type V IF-protein, the Caenorhabditis elegans nuclear lamin (Ce-lamin), is a promising building block for protein-based fibers. Electron cryo-tomography of vitrified sections enabled us to depict the higher ordered assembly of the Ce-lamin into macroscopic fibers through the creation of paracrystalline fibers, which are prominent in vitro structures of lamins. The lamin fibers respond to tensile force as other IF-protein-based fibers, i.e., hagfish slime threads, and possess unique mechanical properties that may potentially be used in certain applications. The self-assembly nature of lamin proteins into a filamentous structure, which is further assembled into a complex network, can be easily modulated. This knowledge may lead to a better understanding of the relationship in IF-proteins-based fibers and materials, between their hierarchical structures and their mechanical properties.

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Dragline, Egg Stalk and Byssus: A Comparison of Outstanding Protein Fibers and Their Potential for Developing New Materials

Abstract: This feature article discusses three remarkable protein fi bers: spider dragline, lacewing egg stalk and mussel byssus. Sequence-structure-function relationships of selected proteins in the fi bers are highlighted and the potential of these proteins for use as new materials is summarized.

Cited by 39 publications

References 204 publications

pH‐Responsive Self‐Organization of Metal‐Binding Protein Motifs from Biomolecular Junctions in Mussel Byssus

pH‐Responsive Self‐Organization of Metal‐Binding Protein Motifs from Biomolecular Junctions in Mussel Byssus

The multi-layered protective cuticle of Collembola: a chemical analysis

The assembly of C. elegans lamins into macroscopic fibers

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