Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

Wasko, Stephen Scott; Tay, Gavin; Schwaighofer, Andreas; Nowak, Christoph; Waite, J. Herbert; Miserez, Ali

doi:10.1021/bm401598z

Cited by 20 publications

(24 citation statements)

References 66 publications

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“…Fig. 45a and b shows a channeled whelk (Busycotypus canaliculatus) and its egg capsules [219]. During incubation period ($10 months), the capsules have to protect the delicate embryos from various environmental damages, such as strong hydrodynamic forces generated by water at velocities more than 10 m/s, abrasion from sand, diffusion of poisonous substances, ultraviolet light, and attack from predators [220,221].…”

Section: Whelk Egg Capsulesmentioning

confidence: 99%

“…45. Photographs of (a) a whelk (Busycotypus canaliculatus) and its string of egg capsules and (b) close view of the capsules [219]. Fig.…”

Section: Whelk Egg Capsulesmentioning

confidence: 99%

“…The whelk egg capsule is a robust proteinaceous biopolymer, and studies have found that it possesses an a-helical coiled-coil structure (wide-angle X-ray scattering, sequencing of proteins) and shows multiple laminate sheets of ordered fibrils with periodicities 50 nm [219,222,223], which is structurally analogous to the a-keratinous materials [18,224]. At the nanoscale, the capsule wall shows distinct structural features: it consists of cross-plied or slightly misoriented sheets of protein fibrils (Fig.…”

Section: Whelk Egg Capsulesmentioning

confidence: 99%

“…The whelk egg capsules also show very unique mechanical properties as an effective shock/energy absorber: under extension it undergoes a-helix M b-sheet transition with large and reversible extensibility, and although this suggests of an elastomer that features low modulus, high extensibility, and entropy-driven elastic recovery, the capsule wall recovery is correlated to the internal energy arising from the facile and reversible a M b transition [116,219,226]. Fig.…”

Section: Whelk Egg Capsulesmentioning

confidence: 99%

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Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration

Wang

Yang

McKittrick

et al. 2016

Progress in Materials Science

660

474

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a b s t r a c tA ubiquitous biological material, keratin represents a group of insoluble, usually high-sulfur content and filament-forming proteins, constituting the bulk of epidermal appendages such as hair, nails, claws, turtle scutes, horns, whale baleen, beaks, and feathers. These keratinous materials are formed by cells filled with keratin and are considered 'dead tissues'. Nevertheless, they are among the toughest biological materials, serving as a wide variety of interesting functions, e.g. scales to armor body, horns to combat aggressors, hagfish slime as defense against predators, nails and claws to increase prehension, hair and fur to protect against the environment. The vivid inspiring examples can offer useful solutions to design new structural and functional materials.Keratins can be classified as a-and b-types. Both show a characteristic filament-matrix structure: 7 nm diameter intermediate filaments for a-keratin, and 3 nm diameter filaments for b-keratin.Both are embedded in an amorphous keratin matrix. The molecular unit of intermediate filaments is a coiled-coil heterodimer and that of b-keratin filament is a pleated sheet. The mechanical response of a-keratin has been extensively studied and shows linear Hookean, yield and post-yield regions, and in some cases, a high reversible elastic deformation. Thus, they can be also be considered 'biopolymers'. On the other hand, b-keratin has not been investigated as comprehensively. Keratinous materials are strain-rate sensitive, and the effect of hydration is significant.Keratinous materials exhibit a complex hierarchical structure: polypeptide chains and filament-matrix structures at the nanoscale, Progress in Materials Science 76 (2016) 229-318 Contents lists available at ScienceDirect Progress in Materials Sciencej o u r n a l h o m e p a g e : w w w . e l s e v i e r . c o m / l o c a t e / p m a t s c i organization of keratinized cells into lamellar, tubular-intertubular, fiber or layered structures at the microscale, and solid, compact sheaths over porous core, sandwich or threads at the macroscale. These produce a wide range of mechanical properties: the Young's modulus ranges from 10 MPa in stratum corneum to about 2.5 GPa in feathers, and the tensile strength varies from 2 MPa in stratum corneum to 530 MPa in dry hagfish slime threads. Therefore, they are able to serve various functions including diffusion barrier, buffering external attack, energy-absorption, impact-resistance, piercing opponents, withstanding repeated stress and aerodynamic forces, and resisting buckling and penetration.A fascinating part of the new frontier of materials study is the development of bioinspired materials and designs. A comprehensive understanding of the biochemistry, structure and mechanical properties of keratins and keratinous materials is of great importance for keratin-based bioinspired materials and designs. Current bioinspired efforts including the manufacturing of quill-inspired aluminum composites, animal horn-inspired SiC composites, and feather-i...

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Section: Whelk Egg Capsulesmentioning

confidence: 99%

“…45. Photographs of (a) a whelk (Busycotypus canaliculatus) and its string of egg capsules and (b) close view of the capsules [219]. Fig.…”

Section: Whelk Egg Capsulesmentioning

confidence: 99%

Section: Whelk Egg Capsulesmentioning

confidence: 99%

Section: Whelk Egg Capsulesmentioning

confidence: 99%

See 2 more Smart Citations

Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration

Wang

Yang

McKittrick

et al. 2016

Progress in Materials Science

660

474

View full text Add to dashboard Cite

show abstract

“…They usually consist of different kinds of proteins (such as collagen in shark egg cases : Evans 1981; or silk proteins in spider cocoons: Stubbs et al 1992;Garb & Hayashi 2005), glycoproteins (e.g. egg capsules of marine invertebrates: Westley & Benkendorff 2009;Wasko et al 2014) or calcium carbonate and other minerals (e.g. egg shells of birds; Hincke et al 2012).…”

Section: Postzygotic Coatsmentioning

confidence: 99%

Evolution of egg coats: linking molecular biology and ecology

2015

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One central goal of evolutionary biology is to explain how biological diversity emerges and is maintained in nature. Given the complexity of the phenotype and the multifaceted nature of inheritance, modern evolutionary ecological studies rely heavily on the use of molecular tools. Here, we show how molecular tools help to gain insight into the role of egg coats (i.e. the extracellular structures surrounding eggs and embryos) in evolutionary diversification. Egg coats are maternally derived structures that have many biological functions from mediating fertilization to protecting the embryo from environmental hazards. They show great molecular, structural and functional diversity across species, but intraspecific variability and the role of ecology in egg coat evolution have largely been overlooked. Given that much of the variation that influences egg coat function is ultimately determined by their molecular phenotype, cutting-edge molecular tools (e.g. proteomics, glycomics and transcriptomics), combined with functional assays, are needed for rigorous inferences on their evolutionary ecology. Here, we identify key research areas and highlight emerging molecular techniques that can increase our understanding of the role of egg coats in the evolution of biological diversity, from adaptation to speciation.

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Stimuli‐Responsive Natural Proteins and Their Applications

Sun

et al. 2021

ChemBioChem

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Natural proteins are essential biomacromolecules that fulfill versatile functions in the living organism, such as their usage as cytoskeleton, nutriment transporter, homeostasis controller, catalyzer, or immune guarder. Due to the excellent mechanical properties and good biocompatibility/biodegradability, natural protein-based biomaterials are well equipped for prospective applications in various fields. Among these natural proteins, stimuli-responsive proteins can be reversibly and precisely manipulated on demand, rendering the protein-based biomate-rials promising candidates for numerous applications, including disease detection, drug delivery, bio-sensing, and regenerative medicine. Therefore, we present some typical natural proteins with diverse physical stimuli-responsive properties, including temperature, light, force, electrical, and magnetic sensing in this review. The structure-function mechanism of these proteins is discussed in detail. Finally, we give a summary and perspective for the development of stimuli-responsive proteins.

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Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

Cited by 20 publications

References 66 publications

Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration

Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration

Evolution of egg coats: linking molecular biology and ecology

Stimuli‐Responsive Natural Proteins and Their Applications

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