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The Chemical Properties of Silk Raw Materials
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The Chemical Properties of Silk Raw Materials

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Macromolecular Chemistry".

Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 10129

Special Issue Editor

Dr. Peter R. Laity

E-Mail Website
Guest Editor
Department of Materials Science and Engineering, University of Sheffield, Sheffield, UK
Interests: rheology; spectroscopy; polymer science; chemical and physical characterisation; chemical structure-property relations; natural materials

Special Issue Information

Dear Colleagues,

The enigmatic ability of many arthropods (notably spiders and lepidopteran larvae) to spin silk fibres has evoked wonder, provided the basis for a textile industry, and inspired much scientific interest. Natural silk spinning involves the conversion of an aqueous feedstock to insoluble fibres with impressive mechanical properties, under ambient conditions and without the need for environmentally harmful chemicals. Notwithstanding extensive research, however, much of this process remains shrouded in mystery. Indeed, while it is known that protein gelation (from solution to solid) occurs in response to flow, the physical chemistry underlying this phase change remains obscure. This includes the roles played by interactions between different proteins or other chemical species, including metal ions. Moreover, while striking chemical differences can be observed between proteins in different types of spider silks, in silks from different species of spider, or from other silk-producing animals, reasons for these differences are largely unknown. Hence, much of what has been published to date may be unconvincing—or even contradicted by other research.

This Special Issue of Molecules brings together some of the latest research and scientific opinion regarding the fundamental aspects of protein science, in an attempt to provide a clearer understanding of native silk fibre spinning. Topics may include (but are not limited to) the structure of silk proteins in solution, role of hydration in protein solubility, gelation and fibre formation, similarities and differences between silks from different animals, relationships between diet and silk compositions from different animals, importance of the amino acid sequence, the role of acid- and amine-substituted amino acids in the protein, functionality and interactions of terminal segments, recombinant silk proteins, and ‘non-silk’ animal protein exudates.

Dr. Peter R. Laity
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • silk raw materials
  • chemistry of silk raw materials
  • physical chemistry of silk feedstock
  • rheology of native silk feedstock
  • silk composition from different animals
  • structure–property relations of silks
  • chemical and physical characterisation
  • silk gelation and fibre formation

Published Papers (5 papers)

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Research

18 pages, 5682 KiB  
Article
Recombinant Spider Silk Fiber with High Dimensional Stability in Water and Its NMR Characterization
by Tetsuo Asakura, Hironori Matsuda, Akira Naito, Hideyasu Okamura, Yu Suzuki and Yunosuke Abe
Molecules 2022, 27(23), 8479; https://doi.org/10.3390/molecules27238479 - 02 Dec 2022
Viewed by 1384
Abstract
Spider dragline silk has unique characteristics of strength and extensibility, including supercontraction. When we use it as a biomaterial or material for textiles, it is important to suppress the effect of water on the fiber by as much as possible in order to [...] Read more.
Spider dragline silk has unique characteristics of strength and extensibility, including supercontraction. When we use it as a biomaterial or material for textiles, it is important to suppress the effect of water on the fiber by as much as possible in order to maintain dimensional stability. In order to produce spider silk with a highly hydrophobic character, based on the sequence of ADF-3 silk, we produced recombinant silk (RSSP(VLI)) where all QQ sequences were replaced by VL, while single Q was replaced by I. The artificial RSSP(VLI) fiber was prepared using formic acid as the spinning solvent and methanol as the coagulant solvent. The dimensional stability and water absorption experiments of the fiber were performed for eight kinds of silk fiber. RSSP(VLI) fiber showed high dimensional stability, which is suitable for textiles. A remarkable decrease in the motion of the fiber in water was made evident by 13C solid-state NMR. This study using 13C solid-state NMR is the first trial to put spider silk to practical use and provide information regarding the molecular design of new recombinant spider silk materials with high dimensional stability in water, allowing recombinant spider silk proteins to be used in next-generation biomaterials and materials for textiles. Full article
(This article belongs to the Special Issue The Chemical Properties of Silk Raw Materials)
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13 pages, 2013 KiB  
Article
Broadband Multidimensional Spectroscopy Identifies the Amide II Vibrations in Silkworm Films
by Adam S. Chatterley, Peter Laity, Chris Holland, Tobias Weidner, Sander Woutersen and Giulia Giubertoni
Molecules 2022, 27(19), 6275; https://doi.org/10.3390/molecules27196275 - 23 Sep 2022
Cited by 9 | Viewed by 1691
Abstract
We used two-dimensional infrared spectroscopy to disentangle the broad infrared band in the amide II vibrational regions of Bombyx mori native silk films, identifying the single amide II modes and correlating them to specific secondary structure. Amide I and amide II modes have [...] Read more.
We used two-dimensional infrared spectroscopy to disentangle the broad infrared band in the amide II vibrational regions of Bombyx mori native silk films, identifying the single amide II modes and correlating them to specific secondary structure. Amide I and amide II modes have a strong vibrational coupling, which manifests as cross-peaks in 2D infrared spectra with frequencies determined by both the amide I and amide II frequencies of the same secondary structure. By cross referencing with well-known amide I assignments, we determined that the amide II (N-H) absorbs at around 1552 and at 1530 cm–1 for helical and β-sheet structures, respectively. We also observed a peak at 1517 cm−1 that could not be easily assigned to an amide II mode, and instead we tentatively assigned it to a Tyrosine sidechain. These results stand in contrast with previous findings from linear infrared spectroscopy, highlighting the ability of multidimensional spectroscopy for untangling convoluted spectra, and suggesting the need for caution when assigning silk amide II spectra. Full article
(This article belongs to the Special Issue The Chemical Properties of Silk Raw Materials)
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15 pages, 2727 KiB  
Article
Strategies for the Biofunctionalization of Straining Flow Spinning Regenerated Bombyx mori Fibers
by Paloma Lozano-Picazo, Cristina Castro-Domínguez, Augusto Luis Bruno, Alejandro Baeza, Adelia S. Martínez, Patricia A. López, Ángela Castro, Yassmin Lakhal, Elena Montero, Luis Colchero, Daniel González-Nieto, Francisco Javier Rojo, Fivos Panetsos, Milagros Ramos, Rafael Daza, Alfonso M. Gañán-Calvo, Manuel Elices, Gustavo Víctor Guinea and José Pérez-Rigueiro
Molecules 2022, 27(13), 4146; https://doi.org/10.3390/molecules27134146 - 28 Jun 2022
Cited by 1 | Viewed by 1382
Abstract
High-performance regenerated silkworm (Bombyx mori) silk fibers can be produced efficiently through the straining flow spinning (SFS) technique. In addition to an enhanced biocompatibility that results from the removal of contaminants during the processing of the material, regenerated silk fibers may [...] Read more.
High-performance regenerated silkworm (Bombyx mori) silk fibers can be produced efficiently through the straining flow spinning (SFS) technique. In addition to an enhanced biocompatibility that results from the removal of contaminants during the processing of the material, regenerated silk fibers may be functionalized conveniently by using a range of different strategies. In this work, the possibility of implementing various functionalization techniques is explored, including the production of fluorescent fibers that may be tracked when implanted, the combination of the fibers with enzymes to yield fibers with catalytic properties, and the functionalization of the fibers with cell-adhesion motifs to modulate the adherence of different cell lineages to the material. When considered globally, all these techniques are a strong indication not only of the high versatility offered by the functionalization of regenerated fibers in terms of the different chemistries that can be employed, but also on the wide range of applications that can be covered with these functionalized fibers. Full article
(This article belongs to the Special Issue The Chemical Properties of Silk Raw Materials)
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27 pages, 3589 KiB  
Article
Volumetric Scalability of Microfluidic and Semi-Batch Silk Nanoprecipitation Methods
by Saphia A. L. Matthew, Refaya Rezwan, Yvonne Perrie and F. Philipp Seib
Molecules 2022, 27(7), 2368; https://doi.org/10.3390/molecules27072368 - 06 Apr 2022
Cited by 7 | Viewed by 2426
Abstract
Silk fibroin nanoprecipitation by organic desolvation in semi-batch and microfluidic formats provides promising bottom-up routes for manufacturing narrow polydispersity, spherical silk nanoparticles. The translation of silk nanoparticle production to pilot, clinical, and industrial scales can be aided through insight into the property drifts [...] Read more.
Silk fibroin nanoprecipitation by organic desolvation in semi-batch and microfluidic formats provides promising bottom-up routes for manufacturing narrow polydispersity, spherical silk nanoparticles. The translation of silk nanoparticle production to pilot, clinical, and industrial scales can be aided through insight into the property drifts incited by nanoprecipitation scale-up and the identification of critical process parameters to maintain throughout scaling. Here, we report the reproducibility of silk nanoprecipitation on volumetric scale-up in low-shear, semi-batch systems and estimate the reproducibility of chip parallelization for volumetric scale-up in a high shear, staggered herringbone micromixer. We showed that silk precursor feeds processed in an unstirred semi-batch system (mixing time > 120 s) displayed significant changes in the nanoparticle physicochemical and crystalline properties following a 12-fold increase in volumetric scale between 1.8 and 21.9 mL while the physicochemical properties stayed constant following a further 6-fold increase in scale to 138 mL. The nanoparticle physicochemical properties showed greater reproducibility after a 6-fold volumetric scale-up when using lower mixing times of greater similarity (8.4 s and 29.4 s) with active stirring at 400 rpm, indicating that the bulk mixing time and average shear rate should be maintained during volumetric scale-up. Conversely, microfluidic manufacture showed high between-batch repeatability and between-chip reproducibility across four participants and microfluidic chips, thereby strengthening chip parallelization as a production strategy for silk nanoparticles at pilot, clinical, and industrial scales. Full article
(This article belongs to the Special Issue The Chemical Properties of Silk Raw Materials)
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34 pages, 3967 KiB  
Article
Seeking Solvation: Exploring the Role of Protein Hydration in Silk Gelation
by Peter R. Laity and Chris Holland
Molecules 2022, 27(2), 551; https://doi.org/10.3390/molecules27020551 - 16 Jan 2022
Cited by 5 | Viewed by 2353
Abstract
The mechanism by which arthropods (e.g., spiders and many insects) can produce silk fibres from an aqueous protein (fibroin) solution has remained elusive, despite much scientific investigation. In this work, we used several techniques to explore the role of a hydration shell bound [...] Read more.
The mechanism by which arthropods (e.g., spiders and many insects) can produce silk fibres from an aqueous protein (fibroin) solution has remained elusive, despite much scientific investigation. In this work, we used several techniques to explore the role of a hydration shell bound to the fibroin in native silk feedstock (NSF) from Bombyx mori silkworms. Small angle X-ray and dynamic light scattering (SAXS and DLS) revealed a coil size (radius of gyration or hydrodynamic radius) around 12 nm, providing considerable scope for hydration. Aggregation in dilute aqueous solution was observed above 65 °C, matching the gelation temperature of more concentrated solutions and suggesting that the strength of interaction with the solvent (i.e., water) was the dominant factor. Infrared (IR) spectroscopy indicated decreasing hydration as the temperature was raised, with similar changes in hydration following gelation by freezing or heating. It was found that the solubility of fibroin in water or aqueous salt solutions could be described well by a relatively simple thermodynamic model for the stability of the protein hydration shell, which suggests that the affected water is enthalpically favoured but entropically penalised, due to its reduced (vibrational or translational) dynamics. Moreover, while the majority of this investigation used fibroin from B. mori, comparisons with published work on silk proteins from other silkworms and spiders, globular proteins and peptide model systems suggest that our findings may be of much wider significance. Full article
(This article belongs to the Special Issue The Chemical Properties of Silk Raw Materials)
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