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Silk Fibroin Materials 2.0
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Silk Fibroin Materials 2.0

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

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 15604

Special Issue Editor

Dr. Yasumoto Nakazawa

E-Mail Website
Guest Editor
Department of Biotechnology and Life Scinece, Tokyo University of Agriculture and Technology, Koganei, Tokyo, Japan
Interests: silk materials; bio-based materials; tissue engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Silk produced by most insects, such as Lepidoptera (silkworms), Araneae (spiders), and Hymenoptera (ants, bees, and hornets), etc., is a natural fiber with excellent mechanical properties and structural characteristics. Such properties are attributed by the higher-order structure and primary structure. The primary structure of silk is composed of a very simple repetitive domain structure, and this repetitive structure is common to various silks such as spider pull yarn and wild species in addition to silk fibroin produced by B. mori. Spectroscopic studies, such as X-ray and NMR, have clearly indicated that a very strong hydrogen bond network formed from these primary structures constitutes a crystalline region of the silk.

Furthermore, the nature of silk has been dramatically expanded by technological innovations such as processing and modification by various genetic recombination including genome editing. In this way, the utility of silk is not limited to conventional fibers and is also applicable in new fields, such as pharmaceutical/medical devices, cosmetics, etc.

The Special Issue "Silk Fibroin Materials" opened for submissions in 2020 and published 14 original papers and 3 Reviews. In light of the growing demand for silk fibroin in various research fields, we have decided to publish a Special Issue "Silk Fibroin Materials 2.0".

Topics of particular interest include, but are not limited to the following:

  1. Structural analysis of various silks in liquid and solid state
  2. Study on self-aggregation and structure control of silk
  3. Application of silk materials produced from various species
  4. Research on the new use of silk (medical, environment, chemistry, food, etc.)
  5. Research on the new processing method of silks
  6. Research on genetically modified silks
  7. Creation of bioinspired materials based on silks

Dr. Yasumoto Nakazawa
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.

Related Special Issue

Published Papers (5 papers)

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Research

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14 pages, 2211 KiB  
Article
Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR
by Yu Suzuki, Takanori Higashi, Takahiro Yamamoto, Hideyasu Okamura, Takehiro K. Sato and Tetsuo Asakura
Molecules 2022, 27(2), 511; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27020511 - 14 Jan 2022
Cited by 4 | Viewed by 2238
Abstract
Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use [...] Read more.
Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed. Full article
(This article belongs to the Special Issue Silk Fibroin Materials 2.0)
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15 pages, 2425 KiB  
Article
Fractionation of Regenerated Silk Fibroin and Characterization of the Fractions
by Masaaki Aoki, Yu Masuda, Kota Ishikawa and Yasushi Tamada
Molecules 2021, 26(20), 6317; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26206317 - 19 Oct 2021
Cited by 2 | Viewed by 2581
Abstract
The molecular weight (MW) of regenerated silk fibroin (RSF) decreases during degumming and dissolving processes. Although MW and the MW distribution generally affect polymer material processability and properties, few reports have described studies examining the influences of MW and the distribution on silk [...] Read more.
The molecular weight (MW) of regenerated silk fibroin (RSF) decreases during degumming and dissolving processes. Although MW and the MW distribution generally affect polymer material processability and properties, few reports have described studies examining the influences of MW and the distribution on silk fibroin (SF) material. To prepare different MW SF fractions, the appropriate conditions for fractionation of RSF by ammonium sulfate (AS) precipitation process were investigated. The MW and the distribution of each fraction were found using gel permeation chromatography (GPC) and SDS-polyacrylamide electrophoresis (SDS-PAGE). After films of the fractionated SFs formed, the secondary structure, surface properties, and cell proliferation of films were evaluated. Nanofiber nonwoven mats and 3D porous sponges were fabricated using the fractionated SF aqueous solution. Then, their structures and mechanical properties were analyzed. The results showed AS precipitation using a dialysis membrane at low temperature to be a suitable fractionation method for RSF. Moreover, MW affects the nanofiber and sponge morphology and mechanical properties, although no influence of MW was observed on the secondary structure or crystallinity of the fabricated materials. Full article
(This article belongs to the Special Issue Silk Fibroin Materials 2.0)
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10 pages, 2154 KiB  
Article
Egg Case Protein 3: A Constituent of Black Widow Spider Tubuliform Silk
by Mikayla Shanafelt, Camille Larracas, Simmone Dyrness, Ryan Hekman, Coby La Mattina-Hawkins, Taylor Rabara, Wilson Wu and Craig A. Vierra
Molecules 2021, 26(16), 5088; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26165088 - 22 Aug 2021
Cited by 3 | Viewed by 2227
Abstract
Spider silk has outstanding mechanical properties, rivaling some of the best materials on the planet. Biochemical analyses of tubuliform silk have led to the identification of TuSp1, egg case protein 1, and egg case protein 2. TuSp1 belongs to the spidroin superfamily, containing [...] Read more.
Spider silk has outstanding mechanical properties, rivaling some of the best materials on the planet. Biochemical analyses of tubuliform silk have led to the identification of TuSp1, egg case protein 1, and egg case protein 2. TuSp1 belongs to the spidroin superfamily, containing a non-repetitive N- and C-terminal domain and internal block repeats. ECP1 and ECP2, which lack internal block repeats and sequence similarities to the highly conserved N- and C-terminal domains of spidroins, have cysteine-rich N-terminal domains. In this study, we performed an in-depth proteomic analysis of tubuliform glands, spinning dope, and egg sacs, which led to the identification of a novel molecular constituent of black widow tubuliform silk, referred to as egg case protein 3 or ECP3. Analysis of the translated ECP3 cDNA predicts a low molecular weight protein of 11.8 kDa. Real-time reverse transcription–quantitative PCR analysis performed with different silk-producing glands revealed ECP3 mRNA is predominantly expressed within tubuliform glands of spiders. Taken together, these findings reveal a novel protein that is secreted into black widow spider tubuliform silk. Full article
(This article belongs to the Special Issue Silk Fibroin Materials 2.0)
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22 pages, 8534 KiB  
Article
Characterization of a Water-Dispersed Biodegradable Polyurethane-Silk Composite Sponge Using 13C Solid-State Nuclear Magnetic Resonance as Coating Material for Silk Vascular Grafts with Small Diameters
by Takashi Tanaka, Yusuke Ibe, Takaki Jono, Ryo Tanaka, Akira Naito and Tetsuo Asakura
Molecules 2021, 26(15), 4649; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26154649 - 31 Jul 2021
Cited by 2 | Viewed by 2420
Abstract
Recently, Bombyx mori silk fibroin (SF) has been shown to be a suitable material for vascular prostheses for small arteries. In this study, we developed a softer SF graft by coating water-dispersed biodegradable polyurethane (PU) based on polycaprolactone and an SF composite sponge [...] Read more.
Recently, Bombyx mori silk fibroin (SF) has been shown to be a suitable material for vascular prostheses for small arteries. In this study, we developed a softer SF graft by coating water-dispersed biodegradable polyurethane (PU) based on polycaprolactone and an SF composite sponge on the knitted SF vascular graft. Three kinds of 13C solid-state nuclear magnetic resonance (NMR), namely carbon-13 (13C) cross-polarization/magic angle spinning (MAS), 13C dipolar decoupled MAS, and 13C refocused insensitive nuclei enhanced by polarization transfer (r-INEPT) NMR, were used to characterize the PU-SF coating sponge. Especially the 13C r-INEPT NMR spectrum of water-dispersed biodegradable PU showed that both main components of the non-crystalline domain of PU and amorphous domain of SF were highly mobile in the hydrated state. Then, the small-diameter SF artificial vascular grafts coated with this sponge were evaluated through implantation experiments with rats. The implanted PU-SF-coated SF grafts showed a high patency rate. It was confirmed that the inside of the SF grafts was covered with vascular endothelial cells 4 weeks after implantation. These results showed that the water-dispersed biodegradable PU-SF-coated SF graft created in this study could be a strong candidate for small-diameter artificial vascular graft. Full article
(This article belongs to the Special Issue Silk Fibroin Materials 2.0)
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Review

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20 pages, 6580 KiB  
Review
Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix-
by Tetsuo Asakura
Molecules 2021, 26(12), 3706; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26123706 - 17 Jun 2021
Cited by 44 | Viewed by 4683
Abstract
Recently, considerable attention has been paid to Bombyx mori silk fibroin by a range of scientists from polymer chemists to biomaterial researchers because it has excellent physical properties, such as strength, toughness, and biocompatibility. These appealing physical properties originate from the silk fibroin [...] Read more.
Recently, considerable attention has been paid to Bombyx mori silk fibroin by a range of scientists from polymer chemists to biomaterial researchers because it has excellent physical properties, such as strength, toughness, and biocompatibility. These appealing physical properties originate from the silk fibroin structure, and therefore, structural determinations of silk fibroin before (silk I) and after (silk II) spinning are a key to make wider applications of silk. There are discrepancies about the silk I structural model, i.e., one is type II β-turn structure determined using many solid-state and solution NMR spectroscopies together with selectively stable isotope-labeled model peptides, but another is α-helix or partially α-helix structure speculated using IR and Raman methods. In this review, firstly, the process that led to type II β-turn structure by the authors was introduced in detail. Then the problems in speculating silk I structure by IR and Raman methods were pointed out together with the problem in the assignment of the amide I band in the spectra. It has been emphasized that the conformational analyses of proteins and peptides from IR and Raman studies are not straightforward and should be very careful when the proteins contain β-turn structure using many experimental data by Vass et al. In conclusion, the author emphasized here that silk I structure should be type II β-turn, not α-helix. Full article
(This article belongs to the Special Issue Silk Fibroin Materials 2.0)
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