Force-Induced Structural Changes in Spider Silk Fibers Introduced by ATR-FTIR Spectroscopy

Jafari, Mohammad Javad; Bäcklund, Fredrik G.; Arndt, Tina; Schmuck, Benjamin; Greco, Gabriele; Rising, Anna; Barth, Andreas; Ederth, Thomas

doi:10.1021/acsapm.3c01892

Cited by 3 publications

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Sustainable Spinning of Artificial Spider Silk Fibers with Excellent Toughness and Inherent Potential for Functionalization

Fan,

Knuuttila,

Schmuck

et al. 2024

Adv Funct Materials

View full text Add to dashboard Cite

Despite impressive progress in the field, there are still several major bottlenecks in producing fibers from recombinantly produced spider‐silk‐like proteins to replicate the extraordinary mechanical properties of spider major ampullate silk. The conventional artificial fiber spinning processes rely primarily on organic solvents to coagulate proteins into fibers and require complex post‐treatments to obtain fibers with valuable properties. This is due to challenges in obtaining soluble silk proteins, but also because the native silk spinning process leading to the hierarchical organization of the silk proteins is not fully understood and is hard to replicate in a manner applicable to industrial settings. Here, recombinant spider‐silk fusion proteins are efficiently produced and processed into as‐spun fibers with a toughness modulus of 120 MJ m−3 and extensibility of 255% using solely aqueous solutions. The spider‐silk fusion proteins assemble in a manner similar to that reported for native spider silk: they phase separate induced by salting out, followed by alignment and a secondary structure transition triggered by shear forces and dehydration. Finally, the design of the fusion silk proteins enables straightforward functionalization of the fibers under mild all‐aqueous conditions via a simple biomolecular click reaction both pre‐ and post‐spinning.

show abstract

Sustainable Spinning of Artificial Spider Silk Fibers with Excellent Toughness and Inherent Potential for Functionalization

Fan,

Knuuttila,

Schmuck

et al. 2024

Adv Funct Materials

View full text Add to dashboard Cite

show abstract

Structural adaptability and surface activity of peptides derived from tardigrade proteins

Giubertoni,

Chagri,

Argudo

et al. 2024

Protein Science

View full text Add to dashboard Cite

Tardigrades are unique micro‐organisms with a high tolerance to desiccation. The protection of their cells against desiccation involves tardigrade‐specific proteins, which include the so‐called cytoplasmic abundant heat soluble (CAHS) proteins. As a first step towards the design of peptides capable of mimicking the cytoprotective properties of CAHS proteins, we have synthesized several model peptides with sequences selected from conserved CAHS motifs and investigated to what extent they exhibit the desiccation‐induced structural changes of the full‐length proteins. Using circular dichroism spectroscopy, two‐dimensional infrared spectroscopy, and molecular dynamics simulations, we have found that the CAHS model peptides are mostly disordered, but adopt a more ‐helical structure upon addition of 2,2,2‐trifluoroethanol, which mimics desiccation. This structural behavior is similar to that of full‐length CAHS proteins, which also adopt more ordered conformations upon desiccation. We also have investigated the surface activity of the peptides at the air/water interface, which also mimics partial desiccation. Interestingly, sum‐frequency generation spectroscopy shows that all model peptides are surface active and adopt a helical structure at the air/water interface. Our results suggest that amino acids with high helix‐forming propensities might contribute to the propensity of these peptides to adopt a helical structure when fully or partially dehydrated. Thus, the selected sequences retain part of the CAHS structural behavior upon desiccation, and might be used as a basis for the design of new synthetic peptide‐based cryoprotective materials.

show abstract

Upcycling tannery sludge into superior micro/nano protein fibers to reinforce the mechanical and flame retardant properties of cellulose-based film

Wei,

He,

Liu

et al. 2024

Preprint

View full text Add to dashboard Cite

Micro/nano protein fibers have attracted increasing attention owing to their advantageous properties for applications in advanced materials. Traditional preparation methods often suffer from high costs of raw-materials and energy-intensive manufacturing processes, which hinder large-scale production. Herein, we present an innovative low-carbon approach for converting tannery sludge into micro/nano protein fibers. The alkali-oxygen cooking combined with ultrasonic process shown the potential to reduce carbon emissions. The resulting micro/nano protein fibers reinforced the mechanical properties of the cellulose-based films. The maximum tensile force of the cellulose-based film was increased by 55.40%, and the Young’s modulus was increased by 22.92%. The micro/nano protein fibers also imparted remarkable flame-retardant characteristics, as indicated by an increased peak temperature of heat loss and a 21.60% reduction in the peak heat release rate of cellulose-based films. This low-carbon and ecofriendly process utilizing leather tannery sludge not only provides a sustainable source of raw materials but also contributes to the circular economy by repurposing industrial waste.

show abstract

Force-Induced Structural Changes in Spider Silk Fibers Introduced by ATR-FTIR Spectroscopy

Cited by 3 publications

References 63 publications

Sustainable Spinning of Artificial Spider Silk Fibers with Excellent Toughness and Inherent Potential for Functionalization

Sustainable Spinning of Artificial Spider Silk Fibers with Excellent Toughness and Inherent Potential for Functionalization

Structural adaptability and surface activity of peptides derived from tardigrade proteins

Upcycling tannery sludge into superior micro/nano protein fibers to reinforce the mechanical and flame retardant properties of cellulose-based film

Contact Info

Product

Resources

About