Статті в журналах: "Silk fibroin protein"

1

Yang, Ming Ying, Liang Jun Zhu, Si Jia Min, and Tetsuo Asakura. "Synthesis and Characterization of Novel Silk-Like Proteins Using Genetic Engineering Methods." Advanced Materials Research 175-176 (January 2011): 258–65. http://dx.doi.org/10.4028/www.scientific.net/amr.175-176.258.

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Using genetic engineering methods, we attempted to produce novel silk-like proteins with new function by combining several functional sequences selected from fibroin of Bombyx mori (B.mori), Samia Cynthia ricini (S.c.ricini) and spider silks or by inducing cell adhesive sequence or calcium binding sequence into silk proteins. The secondary structure of these silk-like proteins was characterized with solid state NMR. Cell adhesion assay indicated that silk-like proteins have higher cell activity. Mineralization of fibroin protein was improved with induction of calcium binding sequence. Nanofiber formation of silk-like proteins was achieved using electrospinning. Fiber was formed from silk-like proteins. These silk-like proteins might be candidates to meet requirement in the field of biomaterials.

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2

Liu, Junwei, Haowen Sun, Yuwei Peng, Ligen Chen, Wei Xu, and Rong Shao. "Preparation and Characterization of Natural Silk Fibroin Hydrogel for Protein Drug Delivery." Molecules 27, no. 11 (May 25, 2022): 3418. http://dx.doi.org/10.3390/molecules27113418.

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In recent years, hydrogels have been widely used as drug carriers, especially in the area of protein delivery. The natural silk fibroin produced from cocoons of the Bombyx mori silkworm possesses excellent biocompatibility, significant bioactivity, and biodegradability. Therefore, silk fibroin-based hydrogels are arousing widespread interest in biomedical research. In this study, a process for extracting natural silk fibroin from raw silk textile yarns was established, and three aqueous solutions of silk fibroin with different molecular weight distributions were successfully prepared by controlling the degumming time. Silk fibroin was dispersed in the aqueous solution as “spherical” aggregate particles, and the smaller particles continuously accumulated into large particles. Finally, a silk fibroin hydrogel network was formed. A rheological analysis showed that as the concentration of the silk fibroin hydrogel increased its storage modulus increased significantly. The degradation behavior of silk fibroin hydrogel in different media verified its excellent stability, and the prepared silk fibroin hydrogel had good biocompatibility and an excellent drug-loading capacity. After the protein model drug BSA was loaded, the cumulative drug release within 12 h reached 80%. We hope that these investigations will promote the potential utilities of silk fibroin hydrogels in clinical medicine.

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3

Wöltje, Michael, Kristin L. Isenberg, Chokri Cherif, and Dilbar Aibibu. "Continuous Wet Spinning of Regenerated Silk Fibers from Spinning Dopes Containing 4% Fibroin Protein." International Journal of Molecular Sciences 24, no. 17 (August 30, 2023): 13492. http://dx.doi.org/10.3390/ijms241713492.

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The wet spinning of fibers from regenerated silk fibroin has long been a research goal. Due to the degradation of the molecular structure of the fibroin protein during the preparation of the regenerated silk fibroin solution, fibroin concentrations with at least 10% protein content are required to achieve sufficient viscosity for wet spinning. In this study, a spinning dope formulation of regenerated silk fibroin is presented that shows a rheological behavior similar to that of native silk fibroin isolated from the glands of B. mori silkworm larvae. In addition, we present a wet-spinning process that enables, for the first time, the continuous wet spinning of regenerated silk fibroin with only 4% fibroin protein content into an endless fiber. Furthermore, the tensile strength of these wet-spun regenerated silk fibroin fibers per percentage of fibroin is higher than that of all continuous spinning approaches applied to regenerated and native silk fibroin published so far.

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4

Stewart, Russell J., Paul B. Frandsen, Steffen U. Pauls, and Jacqueline Heckenhauer. "Conservation of Three-Dimensional Structure of Lepidoptera and Trichoptera L-Fibroins for 290 Million Years." Molecules 27, no. 18 (September 13, 2022): 5945. http://dx.doi.org/10.3390/molecules27185945.

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The divergence of sister orders Trichoptera (caddisflies) and Lepidoptera (moths and butterflies) from a silk-spinning ancestor occurred around 290 million years ago. Trichoptera larvae are mainly aquatic, and Lepidoptera larvae are almost entirely terrestrial—distinct habitats that required molecular adaptation of their silk for deployment in water and air, respectively. The major protein components of their silks are heavy chain and light chain fibroins. In an effort to identify molecular changes in L-fibroins that may have contributed to the divergent use of silk in water and air, we used the ColabFold implementation of AlphaFold2 to predict three-dimensional structures of L-fibroins from both orders. A comparison of the structures revealed that despite the ancient divergence, profoundly different habitats, and low sequence conservation, a novel 10-helix core structure was strongly conserved in L-fibroins from both orders. Previously known intra- and intermolecular disulfide linkages were accurately predicted. Structural variations outside of the core may represent molecular changes that contributed to the evolution of insect silks adapted to water or air. The distributions of electrostatic potential, for example, were not conserved and present distinct order-specific surfaces for potential interactions with or modulation by external factors. Additionally, the interactions of L-fibroins with the H-fibroin C-termini are different for these orders; lepidopteran L-fibroins have N-terminal insertions that are not present in trichopteran L-fibroins, which form an unstructured ribbon in isolation but become part of an intermolecular β-sheet when folded with their corresponding H-fibroin C-termini. The results are an example of protein structure prediction from deep sequence data of understudied proteins made possible by AlphaFold2.

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5

Lehmann, Tanner, Alyssa E. Vaughn, Sudipta Seal, Kenneth W. Liechty, and Carlos Zgheib. "Silk Fibroin-Based Therapeutics for Impaired Wound Healing." Pharmaceutics 14, no. 3 (March 16, 2022): 651. http://dx.doi.org/10.3390/pharmaceutics14030651.

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Impaired wound healing can lead to local hypoxia or tissue necrosis and ultimately result in amputation or even death. Various factors can influence the wound healing environment, including bacterial or fungal infections, different disease states, desiccation, edema, and even systemic viral infections such as COVID-19. Silk fibroin, the fibrous structural-protein component in silk, has emerged as a promising treatment for these impaired processes by promoting functional tissue regeneration. Silk fibroin’s dynamic properties allow for customizable nanoarchitectures, which can be tailored for effectively treating several wound healing impairments. Different forms of silk fibroin include nanoparticles, biosensors, tissue scaffolds, wound dressings, and novel drug-delivery systems. Silk fibroin can be combined with other biomaterials, such as chitosan or microRNA-bound cerium oxide nanoparticles (CNP), to have a synergistic effect on improving impaired wound healing. This review focuses on the different applications of silk-fibroin-based nanotechnology in improving the wound healing process; here we discuss silk fibroin as a tissue scaffold, topical solution, biosensor, and nanoparticle.

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6

Rattanavises, W., and B. Oonkhanond. "The Gelation Study of Silk Fibroin for Biomedical Application." Advanced Materials Research 506 (April 2012): 385–88. http://dx.doi.org/10.4028/www.scientific.net/amr.506.385.

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Silks are the biomaterials that have been used for a century. Most of them are related to the biomedical applications especially silk fibroin. Since the gelation process of silk fibroin was affected by many factors for example the concentration of silk fibroin protein, pH, temperature and cross-linking agent. These factors also influence on the mechanical properties of the silk gel. This study is then focused on making silk fibroin gel by using poly vinyl alcohol (PVA) as a cross-linking agent and physical induced by ultrasonic. The structure of SF/PVA gel was examined by Fourier Transform Infrared (FT-IR). The two main effects of ultrasonic and PVA to the silk fibroin gelation are the gelation time and the gel structure. The more ultrasonic power and PVA amount can make the silk fibroin solution becomes a gel faster. For the gel structure, both ultrasonic and PVA affect to the Amide I and Amide II structure which lead to the gel characteristic used as a wound dressing in the future.

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7

Lee, Woong-Jin, Kyoungjoo Cho, Aaron-Youngjae Kim, and Gyung-Whan Kim. "Injectable Click Fibroin Bioadhesive Derived from Spider Silk for Accelerating Wound Closure and Healing Bone Fracture." Materials 15, no. 15 (July 30, 2022): 5269. http://dx.doi.org/10.3390/ma15155269.

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Wound closure is a critical step in postoperative wound recovery. Substantial advancements have been made in many different means of facilitating wound closure, including the use of tissue adhesives. Compared to conventional methods, such as suturing, tissue bioadhesives better accelerate wound closure. However, several existing tissue adhesives suffer from cytotoxicity, inadequate tissue adhesive strength, and high costs. In this study, a series of bioadhesives was produced using non-swellable spider silk-derived silk fibroin protein and an outer layer of swellable polyethylene glycol and tannic acid. The gelation time of the spider silk-derived silk fibroin protein bioadhesive is less than three minutes and thus can be used during rapid surgical wound closure. By adding polyethylene glycol (PEG) 2000 and tannic acid as co-crosslinking agents to the N-Hydroxysuccinimide (NHS), and 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) reaction, the adhesive strength of the bioadhesive became 2.5 times greater than that of conventional fibrin glue adhesives. Silk fibroin bioadhesives do not show significant cytotoxicity in vitro compared with other bioadhesives. In conclusion, silk fibroin bioadhesive is promising as a new medical tool for more effective and efficient surgical wound closure, particularly in bone fractures.

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8

Vidya, M., and Senthilkumar Rajagopal. "Silk Fibroin: A Promising Tool for Wound Healing and Skin Regeneration." International Journal of Polymer Science 2021 (October 1, 2021): 1–10. http://dx.doi.org/10.1155/2021/9069924.

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Silk is a functional protein biomaterial produced by a variety of insects like flies, silkworms, scorpions, spiders, and mites. Silk synthesized by silkworms is extensively studied for its applications in tissue engineering and wound healing. Silk is undoubtedly a natural biocompatible material with humans and has its role in medical treatments from ancient times. The silk worm protein comprises two types of proteins namely fibroin and sericin. Silk fibroin makes up approximately 70% of cocoon weight and has wide applications in textiles and in all biomedical applications owing to its biocompatible, nontoxic, biodegradable, less immunogenic, and noncarcinogenic nature. It possesses outstanding toughness and mechanical strength, while silk sericin possesses high defensive ability against ultraviolet light and oxidation. Silk fibroin has been known to induce wound healing by increasing cell proliferation and growth and migrating various types of cells which are involved in different stages of wound healing process. With several silk varieties like silk worm fibroin, silk sericin, recombinant silk materials, and native spider silk have been investigated for its wound healing applications over the last several decades. With an objective of harnessing the silk regenerative properties, plentiful strategies have been studied and applied to develop bioartificial skin grafts and bioactive wound dressings in recent times. This review gives a detailed insight into the structure, general properties, fibroin structure-properties relationship, and biomedical applications of silk fibroin.

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9

Nguyen, Thi Kim Lan, Van Phu Dang, Anh Quoc Le, and Quoc Hien Nguyen. "Research on degradation of silk fibroin by combination of electron beam irradiation and hydrothermal processing." Nuclear Science and Technology 4, no. 2 (June 30, 2014): 42–49. http://dx.doi.org/10.53747/jnst.v4i2.227.

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Silk fibers and silk proteins have been demonstrated to be useful to apply in the textile industry, biomedical, cosmetics, pharmaceuticals. In this study, the effects of electron beam (EB) irradiation combined with hydrothermal processing to the solubility of silk fibroin and generation of soluble silk protein were investigated. The solubility of unirradiated and irradiated fibroin samples were greater than 80 % when hydrothermal degradation was performed in the sodium hydroxide solution at an appropriate concentration of 0.05 M. However, the solubility of irradiated fibroin was greater than that of unirradiated sample. The soluble silk protein content increased from 0.462 to 0.653 mg protein/mg silk fibbroin when irradiation doses increased from 0 to 200 kGy, respectively. The molecular weight of protein was determined by SDS-PAGE method. The characteristics of silk protein were confirmed by scanning electron microscope (SEM), Fourier transform infrared spectroscopy (FT-IR), thermogravimetric analysis (TGA) and X-ray diffraction (XRD).

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10

Wang, Fang, Yingying Li, Christopher R. Gough, Qichun Liu, and Xiao Hu. "Dual-Crystallizable Silk Fibroin/Poly(L-lactic Acid) Biocomposite Films: Effect of Polymer Phases on Protein Structures in Protein-Polymer Blends." International Journal of Molecular Sciences 22, no. 4 (February 13, 2021): 1871. http://dx.doi.org/10.3390/ijms22041871.

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Biopolymer composites based on silk fibroin have shown widespread potential due to their brilliant applications in tissue engineering, medicine and bioelectronics. In our present work, biocomposite nanofilms with different special topologies were obtained through blending silk fibroin with crystallizable poly(L-lactic acid) (PLLA) at various mixture rates using a stirring-reflux condensation blending method. The microstructure, phase components, and miscibility of the blended films were studied through thermal analysis in combination with Fourier-transform infrared spectroscopy and Raman analysis. X-ray diffraction and scanning electron microscope were also used for advanced structural analysis. Furthermore, their conformation transition, interaction mechanism, and thermal stability were also discussed. The results showed that the hydrogen bonds and hydrophobic interactions existed between silk fibroin (SF) and PLLA polymer chains in the blended films. The secondary structures of silk fibroin and phase components of PLLA in composites vary at different ratios of silk to PLLA. The β-sheet content increased with the increase of the silk fibroin content, while the glass transition temperature was raised mainly due to the rigid amorphous phase presence in the blended system. This results in an increase in thermal stability in blended films compared to the pure silk fibroin films. This study provided detailed insights into the influence of synthetic polymer phases (crystalline, rigid amorphous, and mobile amorphous) on protein secondary structures through blending, which has direct applications on the design and fabrication of novel protein–synthetic polymer composites for the biomedical and green chemistry fields.

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11

Brenckle, Mark A., Hu Tao, Sunghwan Kim, Mark Paquette, David L. Kaplan, and Fiorenzo G. Omenetto. "Protein-Protein Nanoimprinting of Silk Fibroin Films." Advanced Materials 25, no. 17 (March 11, 2013): 2409–14. http://dx.doi.org/10.1002/adma.201204678.

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12

G C, Chithrashree, Kumar M S, and Sharada A C. "Sericin, a Versatile Protein from Silkworm - Biomedical Applications." Shanlax International Journal of Arts, Science and Humanities 8, S1-Feb (February 6, 2021): 6–11. http://dx.doi.org/10.34293/sijash.v8is1-feb.3924.

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The silkworm, Bombyx mori, which feeds solely on the leaves of the mulberry plant, produces mulberry silk. The components of Bombyx mori silk are 60-80 percent fibroin, 15-35 percent sericin and 1-5 percent non-sericin, including wax, pigments, sugars and other impurities. Silk sericin is a natural polymer that encloses and holds together two filaments of fibroin in the silk thread used in the cocoon. In the research and production of medical biomaterials and biomedicines, protein-based silk fibroin has been widely used for two decades. Sericin is often neglected and abandoned in the manufacturing of traditional silk fabrics, silk floss or synthetic silk biomaterials as a by-product or waste. However, sericin is not only a highly useful biological substance, but also has a great deal of biological activity, similar to fibroin. General characteristics of both silk proteins, fibroin and sericin, extracted from Bombyx mori silkworm, and the biological activity and possible use of sericin were addressed in this review. Due to its amino acid make-up and antioxidant properties, sericin has been used in the food and cosmetic industry. The moisturizing power provides guidance for wound healing as a therapeutic agent, protection against ultraviolet radiation, and formulation of creams and shampoos. Antioxidant activity associated with low sericin digestibility, which increases application in the medical field, such as antitumor, antimicrobial and anti-inflammatory agent, anticoagulant, works in the health of the colon, enhances constipation and, by improving plasma lipid profile, protects the body from obesity. In addition, the properties of sericin allow its application in tissue engineering and drug delivery as a culture medium and cryopreservation, demonstrating its efficient use as an essential biomaterial.

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13

Ling, Shengjie, Zeming Qi, Zhengzhong Shao, and Xin Chen. "Determination of phase behaviour in all protein blend materials with multivariate FTIR imaging technique." Journal of Materials Chemistry B 3, no. 5 (2015): 834–39. http://dx.doi.org/10.1039/c4tb01808g.

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14

Yang, Won Tae, Kwang Sik Lee, Yeon Jae Hur, Bo Yeon Kim, Jianhong Li, Sibin Yu, Byung Rae Jin, and Doh Hoon Kim. "Spider Silk Fibroin Protein Heterologously Produced in Rice Seeds Reduce Diabetes and Hypercholesterolemia in Mice." Plants 9, no. 10 (September 28, 2020): 1282. http://dx.doi.org/10.3390/plants9101282.

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Silk fibroin proteins are biomaterials with diverse applications. These spider and silkworm proteins have specific biological effects when consumed by mammals; in addition to reducing blood pressure and blood glucose and cholesterol levels, they have anti-human immunodeficiency virus activity. In the present study, rice (Oryza sativa) was engineered to produce the C-terminus of the major ampullate spidroin protein from the spider Araneus ventricosus under the control of a Prolamin promoter. Homozygous transgenic rice lines were identified, and the therapeutic effect of this spider silk fibroin protein on the lipid and glucose metabolism was analyzed in a mouse model. Feeding fat-fed mice, the transgenic rice seeds for four weeks reduced serum concentrations of triglycerides, total cholesterol, low-density lipoprotein cholesterol, glutamic oxaloacetic transaminase, and glutamic pyruvic transaminase, and lowered blood glucose levels. This is the first study to investigate the effects of consumption of rice seeds heterologously expressing spider silk fibroin protein in a mammalian model. Our findings suggest that functional foods containing spider silk fibroin protein might be useful as potential pharmaceutical materials for preventing and treating diabetes, hyperlipidemia, and hypercholesterolemia.

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15

Cheng, Kang, Xiaosheng Tao, Zhenzhen Qi, Zuqiang Yin, Subhas C. Kundu, and Shenzhou Lu. "Highly Absorbent Silk Fibroin Protein Xerogel." ACS Biomaterials Science & Engineering 7, no. 8 (July 26, 2021): 3594–607. http://dx.doi.org/10.1021/acsbiomaterials.1c00467.

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16

Ni, Yusu, Yi Jiang, Kaishi Wang, Zhengzhong Shao, Xin Chen, Shan Sun, Huiqian Yu, and Wen Li. "Chondrocytes cultured in silk-based biomaterials maintain function and cell morphology." International Journal of Artificial Organs 42, no. 1 (October 30, 2018): 31–41. http://dx.doi.org/10.1177/0391398818806156.

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Objective: To characterize the morphology of chondrocytes and the expression and secretion of active collagen II by these cells cultured within a regenerated silk fibroin film. Silk fibroin film cytocompatibility and the effect of silk fibroin on chondrocytes in vitro were also evaluated. Methods: Chondrocytes were transfected with a lentivirus containing a green fluorescent protein marker and cultured within a regenerated silk fibroin film. Effects on chondrocyte adhesion, growth, and expression of functional collagen II were assessed in vitro by analysis with immunofluorescent histochemistry and laser scanning confocal microscopy. Results: The results of this study showed that the regenerated silk fibroin film had no cytotoxic effect on chondrocytes. The regenerated silk fibroin film facilitated the adhesion of chondrocytes with typical morphology. Chondrocytes cultured within silk fibroin films exhibited the expression of collagen II in vitro. Conclusion: Regenerated silk fibroin film was found to be an excellent biomaterial with good cytocompatibility for chondrocytes, because these cells remained functional and maintained normal cell morphology when cultured in silk-based biomaterials. These results suggest that silk-based chondrocyte biomaterial complexes may provide a feasible and functional biomaterial for repairing clinical cartilage defects.

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17

Zhang, Xin, and Zhijuan Pan. "Microstructure Transitions and Dry-Wet Spinnability of Silk Fibroin Protein from Waste Silk Quilt." Polymers 11, no. 10 (October 8, 2019): 1622. http://dx.doi.org/10.3390/polym11101622.

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With excellent biocompatibility and biodegradability, silk fibroin has been developed into many protein materials. For producing regenerated silk fibroin (RSF) fibers, the conformation transition of silk fibroin needs to be thoroughly studied during the spinning process. Since the many silk fabrics that are discarded comprise an increasing waste of resources and increase the pressure on the environment, in this paper, waste silk fiber was recycled in an attempt to prepare regenerated fibroin fiber by dry-wet spinning. Ethanol was the coagulation bath. The rheological properties of all the RSF solutions were investigated to acquire rheology curves and non-Newtonian indexes for spinnability analysis. Four stages of the spinning process were carried out to obtain RSF samples and study their conformation transitions, crystallization, and thermal properties by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction, and differential scanning calorimetry. Quantitative analysis of the FTIR results was performed to obtain specific data regarding the contents of the secondary structures. The results showed that higher concentration spinning solutions had better spinnability. As the spinning process progressed, random coils were gradually converted into β-sheets and crystallization increased. Among the different influencing factors, the ethanol coagulation bath played a leading role in the conformation transitions of silk fibroin.

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18

Wang, Yi Yu, Ying Dong Cheng, Yu Liu, Hui Jing Zhao, and Ming Zhong Li. "The Effect of Ultrasonication on the Gelation Velocity and Structure of Silk Fibroin." Advanced Materials Research 175-176 (January 2011): 143–48. http://dx.doi.org/10.4028/www.scientific.net/amr.175-176.143.

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Silk fibroin hydrogels is an important morphous of biomaterial. As a natural protein collosol, purified native silk fibroin solution can be gelatinized under certain conditions. The main mechanism of the gelation is that the fibroin molecules turn into the β-sheet conformation from the random coils. This transformation of silk fibroin molecules would be influenced by various parameters such as the temperature, pH value, ion concentration and so on. In this paper, the effect of ultrasonication on the gelation velocity and structure of silk fibroin were discussed. It is believed that the cavitations caused by sonication could accelerate the process of gelation of silk fibroin. Our experiments demonstrated that the ultrasonic treatment could greatly reduce the silk fibroin gelation time, especially at a high sonication power exceeding 400W. The results of XRD, FTIR, and Raman spectra indicated that the ultrasonication had no significant effect on the final structure and composition of the silk fibroin gels except the acceleration for the molecular transition from random coil and α-structure to β-sheet conformation of silk fibroin. The SEM images showed freeze-dried fibroin gels close to the ultrasonication source had compact structure, while the structure was more loosening far away to the source.

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Zhang, Weiping, Samual P. Gido, Wayne S. Muller, Stephen A. Fossey, and David L. Kaplan. "A pseudo threefold helical structure found in silk Langmuir-Blodgett films by electron diffraction." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 1216–17. http://dx.doi.org/10.1017/s042482010015191x.

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The high performance tensile properties of silkworm (Bombyx mori) silk fiber has resulted in a long standing interest in the semicrystalline morphology of this material. The properties of silk fiber depend not only on the chemical composition (primary protein structure) but also on the fiber spinning conditions present in the silk gland which induce the formation of a (β-sheet based crystalline morphology (secondary protein structure). Knowledge of the silk structure is essential for understanding how the natural spinning processes results in such excellent material properties, but surprisingly few experimental results are available concerning the detailed structures of silk proteins. Two β-sheet based silk fibroin crystalline structures (e.g. silk I and silk II) have been studied by many authors, but the silk I structure remains largely uncharacterized. Here we report results from thin silk films prepared by the Langmuir-Blodgett (LB) technique which display a new silk fibroin structure with a threefold helical chain conformation.

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20

Baptista, Leandra S., Carolina S. G. Pedrosa, Karina R. da Silva, Ronaldo J. F. C. do Amaral, Michele C. L. Kochem, Hélio Menezes, Aris Sterodimas, José de Faria, Marcio R. R. de Oliveira, and Radovan Borojevic. "Fibroin-Based Material from Natural Silk Can Be Associated with Alginate and Mesenchymal Progenitor Cells." Key Engineering Materials 396-398 (October 2008): 437–40. http://dx.doi.org/10.4028/www.scientific.net/kem.396-398.437.

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Silks are naturally occurring polymers and fibroin, its filament core protein, has been shown to support stem cell differentiation in vitro, and promote tissue repair in vivo. The aim of this study is to develop a biomaterial based on silk-fibroin fibers that can be associated with mesenchymal progenitor cells from human perichondrium in vitro, in order to promote auricular reconstruction in vivo. Silk-fibroin concentrate was dissolved with formic acid solution and freeze-dried in auricular moulds. Fibroin-based material was characterized by scanning electron microscopy and by cytotoxic assays. Perichondrium mesenchymal progenitor cells were characterized by flow cytometry. They expressed the standard mesenchymal stem cell markers, and were able to differentiate into several mesenchymal lineages in vitro. This fibroin-based material is a three-dimensional fibrillar scaffold, non-woven and biocompatible, which was also well integrated with alginate and mesenchymal cells.

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Mazurek, Łukasz, Mateusz Szudzik, Mateusz Rybka, and Marek Konop. "Silk Fibroin Biomaterials and Their Beneficial Role in Skin Wound Healing." Biomolecules 12, no. 12 (December 12, 2022): 1852. http://dx.doi.org/10.3390/biom12121852.

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The skin, acting as the outer protection of the human body, is most vulnerable to injury. Wound healing can often be impaired, leading to chronic, hard-to-heal wounds. For this reason, searching for the most effective dressings that can significantly enhance the wound healing process is necessary. In this regard, silk fibroin, a protein derived from silk fibres that has excellent properties, is noteworthy. Silk fibroin is highly biocompatible and biodegradable. It can easily make various dressings, which can be loaded with additional substances to improve healing. Dressings based on silk fibroin have anti-inflammatory, pro-angiogenic properties and significantly accelerate skin wound healing, even compared to commercially available wound dressings. Animal studies confirm the beneficial influence of silk fibroin in wound healing. Clinical research focusing on fibroin dressings is also promising. These properties make silk fibroin a remarkable natural material for creating innovative, simple, and effective dressings for skin wound healing. In this review, we summarise the application of silk fibroin biomaterials as wound dressings in full-thickness, burn, and diabetic wounds in preclinical and clinical settings.

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22

Qin, Sheng, Lingling Sun, Shu Zhang, Xia Sun, and Muwang Li. "BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori." Insects 13, no. 11 (October 22, 2022): 967. http://dx.doi.org/10.3390/insects13110967.

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Bombyx mori, domesticated from wild silkworms, is an economic insect that feeds on mulberry leaves and produces silk. In the current study, we demonstrated the contribution of BmAbl1 in silk protein synthesis. The inhibition and knockout of BmAbl1 can reduce the larva weight and CSW. The effect on CSW of BmAbl1 is not on the transcriptional level, but on the translational level. RNA-sequencing data suggested that amino acid synthesis and the metabolism process had a great difference between the BmAbl1- and Control strain, particularly glutathione metabolism. An abnormality in glutathione metabolism led to the reduction of free glycine and serine content, which are the main components of fibroin protein. Finally, fibroin protein synthesis has been reduced, including fibroin-heavy chain, fibroin-light chain, and p25 protein. This finding brought to light the role of BmAbl1 in the silk protein synthesis process.

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23

Gosline, J. M., P. A. Guerette, C. S. Ortlepp, and K. N. Savage. "The mechanical design of spider silks: from fibroin sequence to mechanical function." Journal of Experimental Biology 202, no. 23 (December 1, 1999): 3295–303. http://dx.doi.org/10.1242/jeb.202.23.3295.

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Анотація:

Spiders produce a variety of silks, and the cloning of genes for silk fibroins reveals a clear link between protein sequence and structure-property relationships. The fibroins produced in the spider's major ampullate (MA) gland, which forms the dragline and web frame, contain multiple repeats of motifs that include an 8–10 residue long poly-alanine block and a 24–35 residue long glycine-rich block. When fibroins are spun into fibres, the poly-alanine blocks form (β)-sheet crystals that crosslink the fibroins into a polymer network with great stiffness, strength and toughness. As illustrated by a comparison of MA silks from Araneus diadematus and Nephila clavipes, variation in fibroin sequence and properties between spider species provides the opportunity to investigate the design of these remarkable biomaterials.

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Wang, Yu, Beom Joon Kim, Berney Peng, Wenyi Li, Yuqi Wang, Meng Li, and Fiorenzo G. Omenetto. "Controlling silk fibroin conformation for dynamic, responsive, multifunctional, micropatterned surfaces." Proceedings of the National Academy of Sciences 116, no. 43 (October 7, 2019): 21361–68. http://dx.doi.org/10.1073/pnas.1911563116.

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Protein micro/nanopatterning has long provided sophisticated strategies for a wide range of applications including biointerfaces, tissue engineering, optics/photonics, and bioelectronics. We present here the use of regenerated silk fibroin to explore wrinkle formation by exploiting the structure–function relation of silk. This yields a biopolymer-based reversible, multiresponsive, dynamic wrinkling system based on the protein’s responsiveness to external stimuli that allows on-demand tuning of surface morphologies and properties. The polymorphic transitions of silk fibroin enable modulation of the wrinkle patterns and, consequently, the material’s physical properties. The interplay between silk protein chains and external stimuli enables control over the protein film’s wrinkling dynamics. Thanks to the versatility of regenerated silk fibroin as a technological substrate, a number of demonstrator devices of varying utility are shown ranging from information encoding to modulation of optical transparency and thermal regulation.

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Agostini de Moraes, Mariana, Mariana Ferreira Silva, Raquel Farias Weska, and Marisa Masumi Beppu. "Silk Fibroin: A Promising Biomaterial." Advanced Materials Research 409 (November 2011): 99–104. http://dx.doi.org/10.4028/www.scientific.net/amr.409.99.

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Silk fibroin (SF) is a protein fiber spun by Bombyx mori silkworm. SF fibers are about 10-25 μm wide in diameter and a single cocoon may provide over 1000 m of SF fibers. SF can present several conformations regarding protein secondary structure which ultimately define the structural properties of SF-based materials. For this reason, a rigorous control on its processing conditions shall be performed. It is known that SF has excellent properties to be used in biomaterials field, controlled release and scaffolds for tissue engineering. In addition, SF can be processed in several forms, such as films, fibers, hydrogels or microparticles. This work seeks to provide an overview on SF processing conditions, regarding the preparation of SF membranes (dense and porous), hydrogels and biocomposites, focusing on biomaterials application.

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TAKIYA, Shigeharu, Hiroki KOKUBO, and Yoshiaki SUZUKI. "Transcriptional regulatory elements in the upstream and intron of the fibroin gene bind three specific factors POU-M1, Bm Fkh and FMBP-1." Biochemical Journal 321, no. 3 (February 1, 1997): 645–53. http://dx.doi.org/10.1042/bj3210645.

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Анотація:

The transcriptional modulator in the fibroin gene intron is composed of multiple octamer-like AT-rich elements, to which several specific DNA-binding proteins named fibroin-modulator-binding proteins (FMBPs) bind. Three major FMBPs in the silk gland were characterized. Two of them (FMBP-2 and -3) were identified as a Fork head homologue (Bm Fkh) and a POU-domain protein (POU-M1) respectively. These factors were expressed in the silk gland with distinct temporal- and spatial-specificities during late larval development as well as during embryogenesis, and did not correlate directly with fibroin gene expression. The other (FMBP-1) appeared to correlate with the expression of the fibroin gene for temporal- and spatial-specificity. These FMBPs also bind to the elements in the upstream modulator. Transcriptional enhancement by both modulators was inhibited by binding competition for these factors with oligonucleotides. These results suggest that expression of the fibroin gene is controlled by co-ordination of these factors with distinct specificities during silk-gland development.

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Wang, Yu Jun, Kazumi Sanai, and Masao Nakagaki. "A Novel Bioadhesive Protein of Silk Filaments Spun Underwater by Caddisfly Larvae." Advanced Materials Research 79-82 (August 2009): 1631–34. http://dx.doi.org/10.4028/www.scientific.net/amr.79-82.1631.

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Aquatic Larvae of Stenopsychid caddisfly (Stenopsychie marmorata) survive by attaching its catching nets at the bottom of the rocks in the flowing water. It was hypothesized that S. marmorata larva connects small pebbles by producing both silk-like protein and strong adhesive protein simultaneously. A 98 kDa protein（Smap-98k）was identified as an adhesive component by constructing a silk gland –specific cDNA library of S. marmorata. The cDNA sequence of Smap-98k was 2,679 bp long and encoding a 893 amino acids–long open reading frame (ORF) in which the first 19 residues are predict to be the signal peptide. The alignment of the Cys residues indicated the primary structure of this protein to consist of 15 degenerated repeats, each about 50 residues long and contains 6 conserved Cys residues. The Smap-98k was characterized by an abundance of Cys residues and charged amino acids with epidermal growth factor-like (EGF-like) structure. The most common amino acid of this protein was Cys (11.98%), with Pro (9.91%) and Glu (9.26%) following order of magnitude. Cys was assumed to play a role in maintaining the topology of charged amino acids on the molecular surface by intramolecular disulphide-bond formation. The gene was expressed specially in the silk gland similarity to the major silk proteins such like heavy fibroin (H-fibroin) and Light fibroin (L-fibroin) of S. marmorata larvae. The sequence of the protein showed certain homology to the silk-185 kDa of Chironomus pallidivittatus (Midge) which also spin silk underwater. The characterizations of abundance of Cys residues and charged amino acids also shared by Megabalanus rosa cement protein (Mrcp-20k ) and Mytilus galloprovincialis foot protein 2 (Mgfp 2) which both were produced in the marine environment. Although the similarity among Smap-98k, Mrcp-20k and Mgfp 2 sequences were very low, the functional relationship in underwater adhesion of these proteins should be noted.

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Jin, Huan Yu, Yu Liu, Xing Liu, Da Peng Wang, Jian Liu, He Mei Zhang, Chun Yan Zong, et al. "Effect of Gamma Irradiation on the Biocompatibility and Biodegradation of Silk Fibroin In Vivo." Advanced Materials Research 535-537 (June 2012): 2361–64. http://dx.doi.org/10.4028/www.scientific.net/amr.535-537.2361.

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Анотація:

Silk fibroin has been a raw material for many artificial biomaterials for a long term, because of it good mechanical property and fantastic biocompatibility. As a natural protein, it has more excellences than other chemically synthetical materials. In present, silk fibroin is used to manufacture bone repair material, artificial blood vessel, microcapsules and so on. However, silk fibroin-based biomaterial is not good enough in biodegradation. In our research, we exposed the silk fibroin film under the gamma ray irradiation with the doses of 25kGy and 50kGy and implanted the film subsequently on the back of SD rats. At dates (7th, 14th, 28th, 56th, 84th ) after implantation, we got the tissue with the implanted film and had the pathological analysis accordingly. The results show that the immune cells infiltration and inflammation decreased within a month. And the immune reaction decreased more quickly in the 50kGy group. And cracks of the silk fibroin film appeared earlier in the 50kGy group. From above observation, it is indicated that the silk fibroin film with a higher dose had better biocompatibility than others. And the silk biodegradation was accelerated by the higher gamma ray dose. Therefore, we can conclude that the gamma ray is able to improve the biocompatibility of silk fibroin and accelerated the biodegradation of it.

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Mu, Xuan, Jugal Kishore Sahoo, Peggy Cebe, and David L. Kaplan. "Photo-Crosslinked Silk Fibroin for 3D Printing." Polymers 12, no. 12 (December 9, 2020): 2936. http://dx.doi.org/10.3390/polym12122936.

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Анотація:

Silk fibroin in material formats provides robust mechanical properties, and thus is a promising protein for 3D printing inks for a range of applications, including tissue engineering, bioelectronics, and bio-optics. Among the various crosslinking mechanisms, photo-crosslinking is particularly useful for 3D printing with silk fibroin inks due to the rapid kinetics, tunable crosslinking dynamics, light-assisted shape control, and the option to use visible light as a biocompatible processing condition. Multiple photo-crosslinking approaches have been applied to native or chemically modified silk fibroin, including photo-oxidation and free radical methacrylate polymerization. The molecular characteristics of silk fibroin, i.e., conformational polymorphism, provide a unique method for crosslinking and microfabrication via light. The molecular design features of silk fibroin inks and the exploitation of photo-crosslinking mechanisms suggest the exciting potential for meeting many biomedical needs in the future.

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Cong, Jiangshan, Cuicui Tao, Xuan Zhang, Hui Zhang, Tingcai Cheng, and Chun Liu. "Transgenic Ectopic Overexpression of Broad Complex (BrC-Z2) in the Silk Gland Inhibits the Expression of Silk Fibroin Genes of Bombyx mori." Insects 11, no. 6 (June 16, 2020): 374. http://dx.doi.org/10.3390/insects11060374.

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Анотація:

Bombyx mori silk protein genes are strictly turned on and off in different developmental stages under the hormone periodically change. The broad complex (BrC) is a transcription factor mediating 20-hydroxyecdysone action, which plays important roles during metamorphosis. Here, we observed that two isoforms of BmBrC (BmBrC-Z2 and BmBrC-Z4) exhibited contrasting expression patterns with fibroin genes (FibH, FibL and P25) in the posterior silk gland (PSG), suggesting that BmBrC may negatively regulate fibroin genes. Transgenic lines were constructed to ectopically overexpress BmBrC-Z2 in the PSG. The silk protein genes in the transgenic line were decreased to almost half of that in the wild type. The silk yield was decreased significantly. In addition, the expression levels of regulatory factors (BmKr-h1 and BmDimm) response to juvenile hormone (JH) signal were inhibited significantly. Then exogenous JH in the BmBrC-Z2 overexpressed lines can inhibit the expression of BmBrC-Z2 and activate the expression of silk protein genes and restore the silk yield to the level of the wild type. These results indicated that BmBrC may inhibit fibroin genes by repressing the JH signal pathway, which would assist in deciphering the comprehensive regulation mechanism of silk protein genes.

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Toshima, Yoshiyuki. "Unusual protein behavior illustrated with silk fibroin." Biochimica et Biophysica Acta (BBA) - Biomembranes 1713, no. 1 (July 2005): 1–4. http://dx.doi.org/10.1016/j.bbamem.2005.05.004.

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Liu, Qiang, Nan Jiang, Dewen Liu, Guoliang Ying, Qiusheng Shi, Ali K. Yetisen, Haifeng Liu, and Yubo Fan. "Monodispersed silk fibroin microdroplets for protein stabilization." Applied Physics Letters 112, no. 17 (April 23, 2018): 173701. http://dx.doi.org/10.1063/1.5026759.

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Tsuboi, Yasuyuki, Hisanori Adachi, Kazushi Yamada, Hiroshi Miyasaka, and Akira Itaya. "Laser Ablation of Silk Protein (Fibroin) Films." Japanese Journal of Applied Physics 41, Part 1, No. 7A (July 15, 2002): 4772–79. http://dx.doi.org/10.1143/jjap.41.4772.

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Samal, Sangram K., David L. Kaplan, and Emo Chiellini. "Ultrasound Sonication Effects on Silk Fibroin Protein." Macromolecular Materials and Engineering 298, no. 11 (May 7, 2013): 1201–8. http://dx.doi.org/10.1002/mame.201200377.

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Zhu, Lei, Junxiong Lin, Liujun Pei, Yuni Luo, Dali Li, and Zhichao Huang. "Recent Advances in Environmentally Friendly and Green Degumming Processes of Silk for Textile and Non-Textile Applications." Polymers 14, no. 4 (February 9, 2022): 659. http://dx.doi.org/10.3390/polym14040659.

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Silk has been widely used not only in the textile field but also in non-textile applications, which is composed of inner fibrous protein, named fibroin, and outer global protein, named sericin. Due to big differences, such as appearance, solubility, amino acid composition and amount of reactive groups, silk fibroin and sericin usually need to be separated before further process. The residual sericin may influence the molecular weight, structure, morphology and properties of silk fibroin, so that degumming of silk is important and necessary, not only in textile field but also in non-textile applications. Traditional textile degumming processes, including soap, alkali or both, could bring such problems as environmental damage, heavy use of water and energy, and damage to silk fibroin. Therefore, this review aims to present a systematic work on environmentally friendly and green degumming processes of raw silk, including art of green degumming process, quantitative and qualitative evaluation, influence of degumming on molecular weight, structure, morphology and properties of silk. It is anticipated that rational selection and design of environmentally friendly and green degumming process is quite important and meaningful, not only for textile application but also for non-textile application.

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Singh, Raunak Raj, Manash Pratim Sarma, Mrinmoy Basak, and Ritismita Devi. "Characterization of Antheraea assamensis Cocoon Proteins as a Potential Candidate against Urinary Tract Infection." Biosciences Biotechnology Research Asia 20, no. 2 (June 30, 2023): 697–701. http://dx.doi.org/10.13005/bbra/3124.

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ABSTRACT: Silk is a biomaterial which is a fibrous protein with remarkable mechanical properties produced in fibre formed by silkworms and spiders. Apart from being a fine biomaterial, it has also been used since past few centuries as sutures in medical surgeries due to its advantages in healing properties and antimicrobial activity to avoid infection. Silk as a material has also been successful in various modern medical areas.1 Here the researchers attempt to study the antimicrobial properties of silk proteins and their potential utility as medicinal agents against the bacteria of the urinary tract infections. This study was done to analyse the affect of muga silk based protein sericin and fibroin on the pathogenic bacteria causing UTI and its role in antibiotic sensitivity. It was found that there was a potential in both the silk proteins (Sericin and fibroin) in its anti-microbial effects against the UTI causing bacteria and had formidable results when treated against them.

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Singh, Vandana, Devika Srivastava, Prashant Pandey, Mukesh Kumar, Sachin Yadav, Dinesh Kumar, and R. Venkatesh Kumar. "Characterization, antibacterial and anticancer study of silk fibroin hydrogel." Journal of Drug Delivery and Therapeutics 13, no. 2 (February 15, 2023): 21–31. http://dx.doi.org/10.22270/jddt.v13i2.5733.

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Purpose: Protein-based hydrogels such as silk fibroin hydrogel, are used in tissue engineering and regenerative medicine applications as they showed striking characteristics like biocompatibility and offered various benefits as biomaterials. The current study sought to prepare silk fibroin hydrogel and characterise it in order to assess its antibacterial and anticancer activity. Methodology: Silk fibroin hydrogel was prepared and characterized by using different microscopy methods, namely Scanning Electron Microscopy (SEM), Phase Contrast Electron (PCM) microscopy, and foldscope analysis. Further, it was characterized through 1H-NMR analysis, Fourier Transform Infrared spectroscopy (FTIR) analysis, and swelling properties. A Current study also covers an antimicrobial and anticancer analysis of silk fibroin hydrogel by disk diffusion method and SRB (Sulforhodamine B) assay respectively. Results: The antibacterial study confirmed that SF hydrogel has a moderate antibacterial activity for Streptococcus mutans, and Salmonella typhi. Additionally, the SRB assay test showed that silk fibroin hydrogels had moderate anticancer activity against the human lung cancer cell line (A549). Conclusion: The current study unequivocally demonstrates that silk fibroin hydrogel has antibacterial and anti-cancerous properties, making it a suitable scaffold for future studies that seek to target a specific drug delivery site. Keywords: Silk fibroin; Swelling behaviour; Anticancer; Drug carrier; Wound healing

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Mitropoulos, Alexander, F. Burpo, Chi Nguyen, Enoch Nagelli, Madeline Ryu, Jenny Wang, R. Sims, Kamil Woronowicz, and J. Wickiser. "Noble Metal Composite Porous Silk Fibroin Aerogel Fibers." Materials 12, no. 6 (March 18, 2019): 894. http://dx.doi.org/10.3390/ma12060894.

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Nobel metal composite aerogel fibers made from flexible and porous biopolymers offer a wide range of applications, such as in catalysis and sensing, by functionalizing the nanostructure. However, producing these composite aerogels in a defined shape is challenging for many protein-based biopolymers, especially ones that are not fibrous proteins. Here, we present the synthesis of silk fibroin composite aerogel fibers up to 2 cm in length and a diameter of ~300 μm decorated with noble metal nanoparticles. Lyophilized silk fibroin dissolved in hexafluoro-2-propanol (HFIP) was cast in silicon tubes and physically crosslinked with ethanol to produce porous silk gels. Composite silk aerogel fibers with noble metals were created by equilibrating the gels in noble metal salt solutions reduced with sodium borohydride, followed by supercritical drying. These porous aerogel fibers provide a platform for incorporating noble metals into silk fibroin materials, while also providing a new method to produce porous silk fibers. Noble metal silk aerogel fibers can be used for biological sensing and energy storage applications.

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Opálková Šišková, Alena, Erika Kozma, Andrej Opálek, Zuzana Kroneková, Angela Kleinová, Štefan Nagy, Juraj Kronek, Joanna Rydz, and Anita Eckstein Andicsová. "Diclofenac Embedded in Silk Fibroin Fibers as a Drug Delivery System." Materials 13, no. 16 (August 13, 2020): 3580. http://dx.doi.org/10.3390/ma13163580.

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Анотація:

Silk fibroin is a biocompatible, non-toxic, mechanically robust protein, and it is commonly used and studied as a material for biomedical applications. Silk fibroin also gained particular interest as a drug carrier vehicle, and numerous silk formats have been investigated for this purpose. Herein, we have prepared electrospun nanofibers from pure silk fibroin and blended silk fibroin/casein, followed by the incorporation of an anti-inflammatory drug, diclofenac. Casein serves as an excipient in pharmaceutical products and has a positive effect on the gradual release of drugs. The characteristics of the investigated composites were estimated by scanning electron microscope, transmission electron microscope, thermogravimetric analysis, and a lifetime of diclofenac by electron paramagnetic resonance analysis. The cumulative release in vitro of diclofenac sodium salt, together with the antiproliferative effect of diclofenac sodium salt-loaded silk nanofibers against the growth of two cancer cell lines, are presented and discussed.

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Long, Shihe, Yun Xiao, and Xingdong Zhang. "Progress in Preparation of Silk Fibroin Microspheres for Biomedical Applications." Pharmaceutical Nanotechnology 8, no. 5 (November 19, 2020): 358–71. http://dx.doi.org/10.2174/2211738508666201009123235.

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: As a natural biomaterial, silk fibroin (SF) holds great potential in biomedical applications with its broad availability, good biocompatibility, high mechanical strength, ease of fabrication, and controlled degradation. With emerging fabrication methods, nanoand microspheres made from SF have brought about unique opportunities in drug delivery, cell culture, and tissue engineering. For these applications, the size and distribution of silk fibroin particles (SFPs) are critical and require precise control during fabrication. Herein, we review common and emerging SFPs fabrication methods and their biomedical applications, and also the challenges and opportunities for SFPs in the near future. : Lay Summary: The application of silk in textile has an extraordinarily long history and new biomedical applications emerged owing to the good biocompatibility and versatile fabrication options of its major protein component, silk fibroin. With the development of nanotechnology and microfabrication, silk fibroin has been fabricated into nano- or microspheres with precisely controlled shape and distribution. In this review, we summarize common and emerging silk fibroin particle fabrication methods and their biomedical applications, and also discuss their challenges and opportunities in the nearest future.

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Kang, Min Sung, Seok Ho Yoon, and Hyoung Joon Jin. "Preparation of Electrospun Protein Nanofibers with Multiwalled Carbon Nanotubes." Key Engineering Materials 326-328 (December 2006): 1737–40. http://dx.doi.org/10.4028/www.scientific.net/kem.326-328.1737.

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A simple and mass producible method was developed to incorporate multiwalled carbon nanotubes (MWCNTs) into electrospun silk fibroin (Bombyx mori) nanofibers. The process consists of dispersing the acid-treated MWCNTs in an aqueous silk fibroin solution, and blending this solution with a water-soluble polymer, poly(ethylene oxide) (PEO), followed by electrospinning of the composite solution. The morphology and microstructure of the electrospun nanofibers were characterized using field emission scanning electron microscopy (FESEM) and transmission electron microscopy (TEM). The FESEM and TEM images show that the MWCNTs are embedded along the nanofibers. Aqueous-based electrospinning of silk/PEO/MWCNTs composites provides potentially useful options for the fabrication of biomaterial scaffolds, e.g. wound dressings, based on this unique fibrous protein.

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Zhu, Huajun, Chunyu Qian, Wanshu Xiao, Qiang Zhang, and Zili Ge. "Performance of a porous composite scaffold containing silk fibroin: Applied research repair on oral jaw epithelial defects." Materials Express 10, no. 4 (April 1, 2020): 490–502. http://dx.doi.org/10.1166/mex.2020.1668.

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Анотація:

Application research on repairing oral and maxillofacial epithelial defects with filin-protein porous composite scaffold. The silk fibroin solution was synthesized by hydrothermal synthesis, and the film was prepared by stirring and pouring. Then silk fibroin film and silk fibroin freeze-dried support were prepared by stirring and smooth casting. It was characterized by FTIR, mechanical properties, dissolution detection, contact Angle and SEM. To evaluate the performance of this material in repairing rabbit oral mucosa and rabbit skin epithelial defects. The characterization shows that the material has good contact Angle, mechanical properties, dissolution and biocompatibility. It has good repair function to rabbit oral epithelial tissue and skin epithelial tissue. Silk fibroin has excellent and unique properties. It has good development prospects and great clinical value in tissue regeneration.

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Echeverri-Correa, Estefanía, David Orlando Grajales-Lopera, Santiago Gutiérrez-Restrepo, and Claudia Patricia Ossa-Orozco. "Effective sericin-fibroin separation from Bombyx mori silkworms fibers and low-cost salt removal from fibroin solution." Revista Facultad de Ingeniería Universidad de Antioquia, no. 94 (October 17, 2019): 97–101. http://dx.doi.org/10.17533/udea.redin.20190731.

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Анотація:

Silk from Bombyx mori has two main proteins: fibroin and sericin. Fibroin is a protein that exhibits good biocompatibility and high surface reactivity, desirable properties for many biomedical applications. Sericin is related with adverse immune response in some medical uses. Therefore, its removal (degumming) is desirable in almost all fields, including the textile industry and biological applications. In this study, three degumming methods (distilled water, liquid neutral detergent and sodium carbonate solution) were evaluated using Raman spectroscopy. Degummed silk treated with sodium carbonate solution exhibits a pattern consistent with previous studies for sericin-free fibroin, and significant differences with the untreated silk pattern. Also, degummed fibroin fibers were dissolved in a calcium chloride solution, in pursuit of a more versatile material. Additionally, different porous membranes of dialysis tubes were tested to remove residual salts, and were compared by conductivity measurements and EDS analysis, identifying good performance for an affordable food cellulose membrane. The results showed that it is possible to obtain fibroin with adequate chemical properties, using low-cost process and membrane of dialysis tubes.

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Lv, Shanshan. "Silk Fibroin-Based Materials for Catalyst Immobilization." Molecules 25, no. 21 (October 24, 2020): 4929. http://dx.doi.org/10.3390/molecules25214929.

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Silk fibroin is a widely and commercially available natural protein derived from silkworm cocoons. Thanks to its unique amino acid composition and structure, which lead to localized nanoscale pockets with limited but sufficient hydration for protein interaction and stabilization, silk fibroin has been studied in the field of enzyme immobilization. Results of these studies have demonstrated that silk fibroin offers an important platform for covalent and noncovalent immobilization of enzymes through serving as a stabilization matrix/support with high retention of the biological activity of the enzymes of interest. In the hope of providing suggestions for potential future research directions, this review has been written to briefly introduce and summarize key advances in silk fibroin-based materials for immobilization of both enzymes/biocatalysts (including alkaline phosphatase, β-glucosidase, glucose oxidase, lipase, urease, uricase, horseradish peroxidase, catalase, xanthine oxidase, tyrosinase, acetylcholinesterase, neutral protease, α-chymotrypsin, amylase, organophosphorus hydrolase, β-galactosidase, carbonic anhydrase, laccase, zymolyase, phenylalanine ammonia-lyase, thymidine kinase, and several others) and non-enzymatic catalysts (such as Au, Pd, Fe, α-Fe2O3, Fe3O4, TiO2, Pt, ZnO, CuO, Cu2O, Mn3O4, and MnO2).

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Levin, B., S. L. Redmond, R. Rajkhowa, R. H. Eikelboom, M. D. Atlas, and R. J. Marano. "Utilising silk fibroin membranes as scaffolds for the growth of tympanic membrane keratinocytes, and application to myringoplasty surgery." Journal of Laryngology & Otology 127, S1 (August 15, 2012): S13—S20. http://dx.doi.org/10.1017/s0022215112001661.

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AbstractBackground:Chronic tympanic membrane perforations can cause significant morbidity. The term myringoplasty describes the operation used to close such perforations. A variety of graft materials are available for use in myringoplasty, but all have limitations and few studies report post-operative hearing outcomes. Recently, the biomedical applications of silk fibroin protein have been studied. This material's biocompatibility, biodegradability and ability to act as a scaffold to support cell growth prompted an investigation of its interaction with human tympanic membrane keratinocytes.Methods and materials:Silk fibroin membranes were prepared and human tympanic membrane keratinocytes cultured. Keratinocytes were seeded onto the membranes and immunostained for a number of relevant protein markers relating to cell proliferation, adhesion and specific epithelial differentiation.Results:The silk fibroin scaffolds successfully supported the growth and adhesion of keratinocytes, whilst also maintaining their cell lineage.Conclusion:The properties of silk fibroin make it an attractive option for further research, as a potential alternative graft in myringoplasty.

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Cai, Jiangyu, Li Zhang, Jun Chen, and Shiyi Chen. "Silk fibroin coating through EDC/NHS crosslink is an effective method to promote graft remodeling of a polyethylene terephthalate artificial ligament." Journal of Biomaterials Applications 33, no. 10 (March 18, 2019): 1407–14. http://dx.doi.org/10.1177/0885328219836625.

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Anterior cruciate ligament reconstruction using polyethylene terephthalate artificial ligaments is one of the research hotspots in sports medicine but it is still challenging to achieve biological healing. The purpose of this study was to modify polyethylene terephthalate ligament with silk fibroin through ethyl-3–(3-dimethylaminopropyl)carbodiimide (EDC)/N-hydroxysuccinimide (NHS) crosslink and to investigate the performance of graft remodeling in vitro and in vivo. After silk fibroin coating, changes in the surface properties of ligament were characterized by scanning electron microscopy, attenuated total reflectance-Fourier transform infrared spectroscopy and water contact angle measurements. The compatibility of polyethylene terephthalate ligament with silk fibroin coating was investigated in vitro. The results showed the silk fibroin coating significantly improved adhesion, proliferation and extracellular matrix secretion of fibroblast cells. Moreover, a rabbit anterior cruciate ligament reconstruction model was established to evaluate the effect of ligament with silk fibroin coating in vivo. The gross observation and histological results showed that the silk fibroin coating significantly inhibited inflammation response and promoted new tissue regeneration with fusiform cells infiltration in and around the graft. Furthermore, the expressions of collagen I protein and mRNA in the silk fibroin-coated polyethylene terephthalate group were much higher than those in the control group according to the immunohistochemical and real-time polymerase chain reaction results. Therefore, silk fibroin coating through EDC/NHS crosslink promotes the biocompatibility and remodeling process of polyethylene terephthalate artificial ligament in vitro and in vivo. It can be considered as a potential solution to the problem of poor remodeling of artificial ligaments after anterior cruciate ligament reconstruction in the clinical applications.

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Mammedzade, A., Ay Mammadova, and O. Gasymov. "STRUCTURE OF SILK FIBROIN NANOPARTICLES: CHARACTERIZATION OF HYDROPHOBIC PATCHES." Russian Journal of Biological Physics and Chemisrty 7, no. 2 (November 15, 2022): 268–72. http://dx.doi.org/10.29039/rusjbpc.2022.0513.

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Nanoparticles are extensively used in various areas of industry. Among different nanoparticles, protein nanoparticles complexed with a wide range of drugs have a great potential for biomedical applications. Silk fibroin exhibits good biocompatibility properties and, therefore, is a good raw material for a wide variety of applications. In this study, structure and hydrophobic patch formation were studied in nanoparticles fabricated from silk fibroin. Far-UV circular dichroism spectroscopy and birefringence observed in a polarized microscope with Congo red staining indicate that fibroin nanoparticles are composed of small amyloid domains. Steady-state and time-resolved fluorescence of ANS revealed two hydrophobic patch formations. Decay-associated spectra of ANS bound to these patches show two species with lifetimes of about 4.2 ns and 14.8 ns. Dissociation constants for ANS complex formation for these patches are 8.3±0.4 M and 5.9±0.3 M, respectively. Acrylamide fluorescence quenching shows that solvent accessibility to native Trp residues is significantly decreased during fibroin nanoparticle formation. Data indicate that nanoparticles fabricated from fibroin are a good candidate for drug delivery applications.

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48

Laity, Peter R., and Chris Holland. "Seeking Solvation: Exploring the Role of Protein Hydration in Silk Gelation." Molecules 27, no. 2 (January 16, 2022): 551. http://dx.doi.org/10.3390/molecules27020551.

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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.

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Crain, Christopher Alan, Nicholas A. Strange, and J. Z. Larese. "Inelastic Neutron Scattering Studies of Natural Silkworm Proteins." MRS Proceedings 1793 (2015): 41–46. http://dx.doi.org/10.1557/opl.2015.658.

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ABSTRACTUnderstanding the interaction of water with biological materials is of fundamental importance. One of main driving forces behind the renewed activity of biomimetic materials involves the dramatic physical properties that many of them exhibit. Two main factors that are critical for understanding silks: the nanoscale semi-crystalline folding structure, and the degree of hydration of the disordered fraction. We describe our investigation of the preparation, characterization and inelastic neutron scattering (INS) studies of the microscopic dynamics of natural Bombyx mori silk fibroin proteins derived from silkworm cocoons. An in situ quartz microbalance is used for monitoring/controlling the hydration and solvent levels of the proteins electrospun onto neutron sample holders. By employing these novel methods our INS investigation facilitated a snapshot of the microscopic silk protein dynamics heretofore not investigated or reported. Preliminary INS measurements illustrate the effect of water and methanol interaction on the dynamics of the fibroin β-pleated sheet component. Evidence of what appears to be a water component (intersheet) distinct from bulk water is clearly apparent in the INS spectrum when the dynamical response from the dry silk is subtracted away.

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50

Bai, Meng-Yi, Meng-Chuan Chen, Wen-Chun Yu, and Jia-Ying Lin. "Foam dressing incorporating herbal extract: An all-natural dressing for potential use in wound healing." Journal of Bioactive and Compatible Polymers 32, no. 3 (November 23, 2016): 293–308. http://dx.doi.org/10.1177/0883911516672240.

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Silk fibroin protein, gastrodia elata, and tea tree oil are naturally derived and have been used throughout human history. This work develops an all-natural and highly porous foam-containing silk fibroin protein and above herbal extract, as a dressing for wound management. Scanning electron microscopic analyses and measurements of porosity by Archimedes method revealed a highly porous structure with porosity ranging from 40%–80%, depending on the preparation condition. In vitro, cytotoxicity test of a series of gastrodia elata–containing silk fibroin protein and tea tree oil–containing silk fibroin protein foam dressings on 3T3 fibroblast cells showed 90%–100% cell viability, which indicated that the produced all-natural dressings have no significant cytotoxicity toward skin cells. In another anti-inflammatory assay using the lipopolysaccharide-induced inflammatory Raw 264.7 macrophages model, the produced two dressings exhibited up to 70% and 90.1% of reduction in the formation of nitrite, in comparison with the untreated group. In vivo studies showed that all herbal extract–containing foam dressings accelerated wound recovery and achieved full closure of the wound within 21 days, and the histological analysis of regenerative skin tissues indicated that the produced foam dressings enhance the generation of thicker, denser, and more abundant collagen fibers in the dermis layer in comparison with the positive and negative control groups.

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