Deployment of hagfish slime thread skeins requires the transmission of mixing forces<i>via</i>mucin strands

Winegard, Timothy M.; Fudge, Douglas S.

doi:10.1242/jeb.038075

Cited by 42 publications

(75 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This indicates that the matrix helps the IFs to resist swelling and maintain high stiffness and strength [124]. In addition, the mechanical properties of dry threads are comparable to those of hydrated hard a-keratinous materials, e.g.…”

Section: Hagfish Slime Threadsmentioning

confidence: 86%

“…There are also studies on fibers composed of matrix-free IF bundles (hagfish slime threads) [115,124]. Interestingly, they reveal that in the absence of matrix proteins, the IF bundles show mechanical properties with more significant hydration sensitivity than a-keratinous materials with matrix proteins (detailed in Section 3.1.8).…”

Section: Hydration Sensitivitymentioning

confidence: 99%

“…43b). The process has been studied and proposed as consisting of the following steps [124,216]: slime exudate is expulsed into convectively mixing seawater; the swelling and elongation of mucin vesicles form mucin strands; these mucin strands attach to the thread skeins and transmit the hydrodynamic forces to the thread skeins, thereby initiating unraveling; entanglement of the threads and mucin strands results in the complete unraveling of thread skeins, forming the whole slime that is a highly complex network of mucin strands (0.0015%), slime threads (0.002%) and seawater (99.996%). Fig.…”

Section: Hagfish Slime Threadsmentioning

confidence: 99%

“…43. Structural characterization of the hagfish slime threads (bundles of keratin IFs): (a) a concentrated exudate (forming the slime) released by the slime glands; it contains both coiled slime threads (skeins) (arrow) and mucin vesicles (arrowheads) that rupture in seawater [216]; (b) differential interference contrast (DIC) image of partially unraveled thread skein in seawater illustrating their coiled structure [124]; (c) DIC image of the whole slime network depicting unraveled threads (arrow) and mucin strands (arrowhead) connecting threads; (d) fluorescence image of the same area in (c) highlighting the mucin network (arrowhead) [124].…”

Section: Hagfish Slime Threadsmentioning

confidence: 99%

“…It is water resistant, and provides shock absorption through adjustable padded straps and full comfort by airflow back channels, durable and protective with personal style. The deployment of hagfish slime thread skeins is interesting since the unraveling from a 150 lm-long bundle to a 100 times longer thread is completed less than a second, and is therefore inspiring [124]. The deployment process has been attributed (Section 3.1.8) to the mucin strands interacting with unraveled slime threads to yield a complex network capable of the viscous entrainment of seawater [124,216].…”

Section: Traditional Bioinspirationmentioning

confidence: 99%

See 4 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

681

474

View full text Add to dashboard Cite

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...

show abstract

Section: Hagfish Slime Threadsmentioning

confidence: 86%

Section: Hydration Sensitivitymentioning

confidence: 99%

Section: Hagfish Slime Threadsmentioning

confidence: 99%

Section: Hagfish Slime Threadsmentioning

confidence: 99%

Section: Traditional Bioinspirationmentioning

confidence: 99%

See 3 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

681

474

View full text Add to dashboard Cite

show abstract

The Internal Structure of the Velvet Worm Projectile Slime: A Small‐Angle Scattering Study

Baer

Hoffmann

Mahmoudi

et al. 2023

Small

View full text Add to dashboard Cite

For prey capture and defense, velvet worms eject an adhesive slime which has been established as a model system for recyclable complex liquids. Triggered by mechanical agitation, the liquid bio‐adhesive rapidly transitions into solid fibers. In order to understand this mechanoresponsive behavior, here, the nanostructural organization of slime components are studied using small‐angle scattering with neutrons and X‐rays. The scattering intensities are successfully described with a three‐component model accounting for proteins of two dominant molecular weight fractions and nanoscale globules. In contrast to the previous assumption that high molecular weight proteins—the presumed building blocks of the fiber core—are contained in the nanoglobules, it is found that the majority of slime proteins exist freely in solution. Only less than 10% of the slime proteins are contained in the nanoglobules, necessitating a reassessment of their function in fiber formation. Comparing scattering data of slime re‐hydrated with light and heavy water reveals that the majority of lipids in slime are contained in the nanoglobules with homogeneous distribution. Vibrating mechanical impact under exclusion of air neither leads to formation of fibers nor alters the bulk structure of slime significantly, suggesting that interfacial phenomena and directional shearing are required for fiber formation.

show abstract

Examples of Bioadhesives for Defence and Predation

Byern

Müller

Voigtländer

et al. 2017

Biologically-Inspired Systems

View full text Add to dashboard Cite

Deployment of hagfish slime thread skeins requires the transmission of mixing forcesviamucin strands

Cited by 42 publications

References 15 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

The Internal Structure of the Velvet Worm Projectile Slime: A Small‐Angle Scattering Study

Examples of Bioadhesives for Defence and Predation

Contact Info

Product

Resources

About