Relevant bibliographies by topics / Silk fibroin protein

Academic literature on the topic 'Silk fibroin protein'

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Published: 6 September 2023

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Journal articles on the topic "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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Silk fibroin protein"

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Kurland, Nicholas. "Design of Engineered Biomaterial Architectures Through Natural Silk Proteins." VCU Scholars Compass, 2013. http://scholarscompass.vcu.edu/etd/571.

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Silk proteins have provided a source of unique and versatile building blocks in the fabrication of biomedical devices for addressing a range of applications. Critical to advancing this field is the ability to establish an understanding of these proteins in their native and engineered states as well as in developing scalable processing strategies, which can fully exploit or enhance the stability, structure, and functionality of the two constituent proteins, silk fibroin and sericin. The research outlined in this dissertation focuses on the evolution in architecture and capability of silks, to effectively position a functionally-diverse, renewable class of silk materials within the rapidly expanding field of smart biomaterials. Study of the process of building macroscopic silk fibers provides insight into the initial steps in the broader picture of silk assembly, yielding biomaterials with greatly improved attributes in the assembled state over those of protein precursors alone. Self-organization processes in silk proteins enable their aggregation into highly organized architectures through simple, physical association processes. In this work, a model is developed for the process of aqueous behavior and aggregation, and subsequent two-dimensional behavior of natural silk sericin, to enable formation of a range of distinct, complex architectures. This model is then translated to an engineered system of fibroin microparticles, demonstrating the role of similar phenomena in creating autonomously-organized structures, providing key insight into future “bottom up” assembly strategies. The aqueous behavior of the water-soluble silk sericin protein was then exploited to create biocomposites capable of enhanced response and biocompatibility, through a novel protein-template strategy. In this work, sericin was added to the biocompatible and biodegradable poly(amino acid), poly(aspartic acid), to improve its pH-dependent swelling response. This work demonstrated the production of a range of porous scaffolds capable providing meaningful response to environmental stimuli, with application in tissue engineering scaffolds and biosensing technologies. Finally, to expand the capabilities of silk proteins beyond process-driven parameters to directly fabricate engineered architectures, a method for silk photopatterning was explored, enabling the direct fabrication of biologically-relevant structures at the micro and nanoscales. Using a facile bioconjugation strategy, native silk proteins could be transformed into proteins with a photoactive capacity. The well-established platform of photolithography could then be incorporated into fabrication strategies to produce a range of architectures capable of addressing spatially-directed material requirements in cell culture and further applications in the use of non-toxic, renewable biological materials.
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Bucciarelli, Alessio. "New methodologies of Silk Proteins processing for advanced applications." Doctoral thesis, Università degli studi di Trento, 2019. http://hdl.handle.net/11572/243375.

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Silk fibroin is a widely studied material in the context of tissue engineering. Thanks to its versatility and impressive properties, the fields where silk fibroin is used have grown. In particular, silk fibroin has proved to be useful in all the cases when an interface with living tissues is needed (e.g. biophotonics, bioelectronics). As a consequence of this increasing interest, a wide range of protocols have been developed to prepare different materials starting from cocoons. The aim of this thesis is to investigate new strategies to fabricate silk fibroin-based materials, either improving previously developed protocols or proposing new methodologies both with the purpose to overcome certain limitations of current approaches and to propose new areas of application. We choose to work on three topics: the production of patterns using photolithography on a fibroin photoresist films (fibroin photocrosslinkable photoresist, FPP), the production of sponges made from a chemically modified version of the native protein (Methacrylated fibroin, Sil-MA), and the production of a solid bulk resin made starting from the regenerated protein. In the case of the FPP (and its counterpart made of sericine, SPP) the fabrication of films and pattern was restricted to the use of harsh chemicals. In addition, the resulting material had a roughness that limits its use in optical applications, making the determination of the refractive index (RI) not possible. The novelty of our work consisted in the modification of the original protocol to make it environmentally sustainable and to decrease the roughness in order to use ellipsometry to determine the RI dispersion. The broadly used silk-based sponges can be prepared by several protocols but they all suffer of the same limitations: the sponges are stabilized only by physical crosslinking (the change from the random to the crystalline secondary structure), and there are no clear models that correlate the sponge properties to their composition. We produced a new sponge, chemically crosslinked, whose stability was ensured by the creation, of chemical bonds between the protein chains during an UV curing. This task was accomplished using a simple protocol and a statistical method to model the composition-properties relations. The possibility to obtain a bulk, non-porous solid monolith from fibroin (solid-fibroin) has been received attention only in the last few years. This material is produced by a transition from solution to solid through solvent evaporation, a very slow process that takes weeks to be completed. The advantage of this transition is that it occurs at room temperature, allowing the addition of thermally degradable molecules (e.g. enzymes). We were able to optimize a procedure to produce the same material by compression of a silk sponge at high pressure and low temperature. The advantage of this method is the lower amount of time required to produce the material, minutes instead of days.
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Bucciarelli, Alessio. "New methodologies of Silk Proteins processing for advanced applications." Doctoral thesis, Università degli studi di Trento, 2019. http://hdl.handle.net/11572/243375.

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Silk fibroin is a widely studied material in the context of tissue engineering. Thanks to its versatility and impressive properties, the fields where silk fibroin is used have grown. In particular, silk fibroin has proved to be useful in all the cases when an interface with living tissues is needed (e.g. biophotonics, bioelectronics). As a consequence of this increasing interest, a wide range of protocols have been developed to prepare different materials starting from cocoons. The aim of this thesis is to investigate new strategies to fabricate silk fibroin-based materials, either improving previously developed protocols or proposing new methodologies both with the purpose to overcome certain limitations of current approaches and to propose new areas of application. We choose to work on three topics: the production of patterns using photolithography on a fibroin photoresist films (fibroin photocrosslinkable photoresist, FPP), the production of sponges made from a chemically modified version of the native protein (Methacrylated fibroin, Sil-MA), and the production of a solid bulk resin made starting from the regenerated protein. In the case of the FPP (and its counterpart made of sericine, SPP) the fabrication of films and pattern was restricted to the use of harsh chemicals. In addition, the resulting material had a roughness that limits its use in optical applications, making the determination of the refractive index (RI) not possible. The novelty of our work consisted in the modification of the original protocol to make it environmentally sustainable and to decrease the roughness in order to use ellipsometry to determine the RI dispersion. The broadly used silk-based sponges can be prepared by several protocols but they all suffer of the same limitations: the sponges are stabilized only by physical crosslinking (the change from the random to the crystalline secondary structure), and there are no clear models that correlate the sponge properties to their composition. We produced a new sponge, chemically crosslinked, whose stability was ensured by the creation, of chemical bonds between the protein chains during an UV curing. This task was accomplished using a simple protocol and a statistical method to model the composition-properties relations. The possibility to obtain a bulk, non-porous solid monolith from fibroin (solid-fibroin) has been received attention only in the last few years. This material is produced by a transition from solution to solid through solvent evaporation, a very slow process that takes weeks to be completed. The advantage of this transition is that it occurs at room temperature, allowing the addition of thermally degradable molecules (e.g. enzymes). We were able to optimize a procedure to produce the same material by compression of a silk sponge at high pressure and low temperature. The advantage of this method is the lower amount of time required to produce the material, minutes instead of days.
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4

Hu, Xiaoyi. "De novo peptide sequencing of spider silk proteins by mass spectrometry and discovery of novel fibroin genes." Scholarly Commons, 2004. https://scholarlycommons.pacific.edu/uop_etds/2734.

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Spiders produce multiple types of silk that exhibit diverse mechanical properties and biological functions. Most molecular studies of spider silk have focused on fibroins from dragline silk and capture silk, two important silk types involved in the survival of the spider. In this study we have focused on the characterization of egg case silk, a third silk fiber produced by the black widow spider, Latrodectus hesperus , whose DNA coding sequences have not been reported. Based upon solubility differences in 8 M guanidine hydrochloride, it is demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and silver staining that the egg case silk is relatively complex at the molecular level, containing a large number of proteins with differing molecular weights. Protein components of egg case silk with a size about 100 kDa were obtained by a solubilization time course study, which indicates these proteins are likely to be embedded in the silk filament. Peptides in these 100 kDa proteins were released by tryptic in-gel and in-solution digestion. The peptides were sequenced using a MALDI tandem TOF mass spectrometer. Some of the de novo sequences were confirmed using a linear ion trap mass spectrometer equipped with a nanospray ion source. Combining the peptide sequences obtained, reverse genetics was employed to trace silk genes encoding proteins containing these de novo peptides. Three silk protein coding sequences were successfully discovered, which encode silk proteins named 3B, T1 and ECSP-1, respectively. 3B and T1 show the standard fibroin protein pattern. Amino acid repeat patterns were observed in these two silk clones. But the amino acid compositions of 3B and T1 show differences with the total amino acid composition of egg case silk, and also, the peptide sequences cannot be found in the primary amino acid sequences of 3B and T1. ECSP-1 protein represents one of the egg case silk proteins with a size of about 100 kDa. A number of peptide sequences obtained by mass spectrometric de novo sequencing were successfully located in ECSP-1's primary amino acid sequence. Sequence analysis demonstrates ECSP-1 represents a new class of silk proteins, with fibroin-like properties. The expression pattern of ecsp-1 is largely restricted to the tubuliform gland inside of the L. hesperus spider, with lower levels detected in the major and minor ampullate glands, which also confirms the identity of ECSP-1. It is also demonstrated that ECSP-1 assembles into higher aggregate structures through the formation of disulfide bonds. Peptide sequences from silk proteins from the Tarantula spider Grammostola rosea were also obtained. These sequences will be beneficial in obtaining genes encoding the silk from this spider species.
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McMullen, Erin. "Characterization of the large diameter fibers in egg case silk : identification of a core fibroin, TuSp1, and localization of fibroin-like molecules, ECPs, from the black widow spider, latrodectus hesperus." Scholarly Commons, 2008. https://scholarlycommons.pacific.edu/uop_etds/704.

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Araneoid spiders use specialized sets of abdominal silk glands to produce up to seven different types of silks, each with diverse functional properties. At the time of these studies, fibroin eDNA sequences that encode egg case silk had not been reported in the literature. This study used conventional nucleic acid-nucleic acid screening of a eDNA library to isolate a novel gene, named tubuliform spidroin 1 , from the black widow spider Latrodectus hesperus. TuSp 1 was demonstrated to be selectively expressed in the tubuliform gland (the gland suspected for egg case silk production), and examination of the amino acid sequence revealed highly homogeneous repeats (184 amino acid ensemble repeats), a characteristic feature of fibroin sequences. Analyses of the ensemble repeats within the amino acid sequence of TuSp 1 revealed the lack of long stretches of polyalanine and glycine-alanine sub-repeats, which are commonly found in minor ampullate and major ampullate silks. Polyserine blocks and short polyalanine stretches were highly represented in the TuSp 1 amino acid sequence. Our data support the assertion that TuSp 1 represents the main constituent within egg case silk. This supposition is supported by the observation that the amino acid composition of raw egg case silk was strikingly similar to the amino acid composition predicted from the translated TuSp1 eDNA. Two additional constituents identified in black widow egg case, egg case protein 1 (ECP-1) and egg case protein 2 (ECP-2), were also partially characterized in this study. Using immunohistochemical approaches, we demonstrate that ECPs predominantly localize to the exterior of the large diameter fibers of egg cases. Additionally, these studies revealed smaller amounts of ECPs localized to the interior portion of the fibers. Collectively, these results support TuSp1 as the predominant fibroin within egg sacs as well as reveal a structural role for the ECPs, providing clues regarding the supramolecular structure of egg case fibers.
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Chuang, Tyler Casey. "Characterization of a family of cysteine rich proteins and development of a MaSp1 derived miniature fibroin." Scholarly Commons, 2014. https://scholarlycommons.pacific.edu/uop_etds/180.

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Spider silk displays a unique balance of high tensile strength and extensibility, making it one of the toughest materials on the planet. Dragline silk, also known as the lifeline of the spider, represents one of the best studied fiber types and many labs are attempting to produce synthetic dragline silk fibers for commercial applications. In these studies, we develop a minifibroin for expression studies in bacteria. Using recombinant DNA methodology and protein expression studies, we develop a natural minifibroin that contains the highly conserved N- and C-terminal domains, along with several internal block repeats of MaSp1. We also characterize a family of small cysteine-rich proteins (CRPs) and demonstrate that these factors are present within the spinning dope of the major ampullate gland using MS analysis. Biochemical studies and characterization of one of the family members, CRP1, demonstrate that this factor can self-polymerize into higher molecular weight complexes under oxidizing conditions, but can be converted into a monomeric species under reducing conditions. Self-polymerization of CRP1 is also shown to be independent of pH and salt concentration, two important chemical cues that help fibroin aggregation. Overall, our data demonstrate that the polymerization state of CRP1 is dependent upon redox state, suggesting that the redox environment during fiber extrusion may help regulate the oligomerization of CRP molecules during dragline silk production.
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7

Guerette, Paul André. "The mechanical properties of spider silk are determined by the genetic regulation of fibroin proteins and chemical and physical processing during spinning." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq25064.pdf.

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Wang, Ting-Teng, and 王鼎騰. "Development of a Silk Fibroin Protein non-woven mat / Silk Sericin Protein foam indicative combination dressing." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/hzuxsx.

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碩士
國立臺灣科技大學
醫學工程研究所
106
In clinical, wound dressing is a necessary medical material to protect and promote wound healing, but postoperative adhesions of dressing cause serious complications in the process of wound healing. It has necessity to provide an dressing material which can reduce requirement of dressing exchange. In this study, we developed an indicative combination dressing which was composed of indicative non-woven and foam dressing. Indicative non-woven mat was fabricated by silk fibroin protein (SFP) and polyvinyl alcohol (PVA) via the single‐spinneret electrospinning technique. The indicative function of non-woven mat was provided by ellagic acid (EA) which is a kind of polyphenols. Foam dressing was an absorbent layer composed of sericin that could control the wettability of wound microenvironment. The indicative function of dressing was attributed to the fluorescence emission which was proved by ascend of UV absorption spectrum and fluorescence emission spectrum. Result of indicative function could be elucidiated by UV absorption spectroscopy, Fourier Transform Infrared Spectrometer and X-ray photoelectron spectroscopy. Our preliminary results indicated that the combination dressing shows potential as a highly hydrophilic, excellent absorptive and low cost wound management material.
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Lin, Sheng-Wei, and 林昇緯. "A hybrid biomaterials combined silk fibroin and mussel protein for biomedical engineering applications." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/85qh69.

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碩士
國立陽明大學
生物醫學工程學系
105
Silk fibroin (SF)-based drug carrier possessed the characteristic of sustain release and pH-sensitive while controlled drug released of SF-based carriers by photothermo effect have yet been investigated. In this study, composite SF film composed of drug-loaded SF-dopamine nanoparticles (SD NPs), bovine serum albumin (BSA) and curcumin were fabricated. SD NPs were first prepared by chemically bonded between tyrosine in SF and catechol of dopamine. BSA and curcumin were then adsorbed onto SD NPs via π-π interaction, respectively. After adsorbing, the particles size of SD NPs, determined by DLS and TEM, increased from 78.3±17.0 nm to 191.3±20.5 nm and 195.6±9.7 nm, respectively. The amount of dopamine in SD NPs were 43.7±2.4 mmole/mmole of SF quantified by Arnow’s assay. Moreover, the release rate of curcu-min can be controlled by SD NPs with two-stage release pattern. After NIR-exposed, both drug release rate of BSA and curcumin increased. Furthermore, this NIR-triggered drug release of composite SF film were enhanced with the increase of the amount of SD NPs. The Young’s modulus of film were 4.2±0.5 MPa after ethanol treatment. Besides, results of anti-coagulation test showed that the film combined with heparin possessed good ability of anticoagulation. In conclusion, the NIR-triggered SD NPs fabricated by simple enzyme catalyzed methods were presented herein. By combining other bio-materials to prepare dual drug-loaded SF-based carriers with photothermo effects may provide a new concept for the design of drug carriers.
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Gil, Eun Seok. "Stimuli-responsive protein-based hydrogels by utilizing [beta]-sheet conformation of silk fibroin as cross-links." 2004. http://www.lib.ncsu.edu/theses/available/etd-12282004-173030/unrestricted/etd.pdf.

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Book chapters on the topic "Silk fibroin protein"

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Yang, Yuejiao, Jie Chen, Claudio Migliaresi, and Antonella Motta. "Natural Fibrous Protein for Advanced Tissue Engineering Applications: Focusing on Silk Fibroin and Keratin." In Advances in Experimental Medicine and Biology, 39–49. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-3258-0_3.

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Cebe, Peggy, Benjamin P. Partlow, David L. Kaplan, Andreas Wurm, Evgeny Zhuravlev, and Christoph Schick. "Fast Scanning Calorimetry of Silk Fibroin Protein: Sample Mass and Specific Heat Capacity Determination." In Fast Scanning Calorimetry, 187–203. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-31329-0_5.

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Andiappan, Muthumanickkam, and Subramanian Sundaramoorthy. "Studies on Indian Eri Silk Electrospun Fibroin Scaffold for Biomedical Applications." In Biomedical Applications of Natural Proteins, 51–64. New Delhi: Springer India, 2015. http://dx.doi.org/10.1007/978-81-322-2491-4_4.

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Yusif Hajibala, Shukurlu, and Huseynov Tokay Maharram. "Increased Morbidity and Its Possible Link to Impaired Selenium Status." In Selenium and Human Health [Working Title]. IntechOpen, 2023. http://dx.doi.org/10.5772/intechopen.110848.

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This chapter summarizes the latest information on the main differences in the chemical properties of selenium proteins and their sulfur analogues, Se proteins and their functions, Se-accumulating proteins, the relationship between Se and hemoglobin, Selenium in gerontology, Selenium and iodine deficiency conditions, Se and immunity, Selenium as an antioxidant in nitrite poisoning. Also discussed are some of the results of the first studies on protein enrichment with selenium carried out in the seventies of the last century. This native protein was natural silk fibroin. Fibroin has since become an important tool for human health and healing. It was discovered that when selenium-containing inorganic compounds were added to mulberry silkworm feed, selenium atoms formed additional sulfur-like bonds in fibroin macromolecules. This resulted in additional branching of protein macromolecule. Selenium atoms in the fibroin structure have a sufficiently high electron affinity, act as small traps and capture migrating electrons. This leads to a reduction of free radicals, which are generated by external influences such as mechanical, thermal, electrical and radiation.
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Omollo Oduor, Edison, Lucy Wanjiru Ciera, and Edwin Kamalha. "Applications of Silk in Biomedical and Healthcare Textiles." In Textiles for Functional Applications. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96644.

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Global trends are shifting towards environmental friendly materials and manufacturing methods. Therefore, natural fiber applications are gaining traction globally. Silk, a natural protein fiber is one of the textile fibers that have recently received more attention due to the new frontiers brought about by technological advancement that has expanded the use of silk fiber beyond the conventional textile industry. The simple and versatile nature of silk fibroin process-ability has made silk appealing in wide range of applications. Silk is biocompatible, biodegradable, easy to functionalize and has excellent mechanical properties, in addition to optical transparency. This review chapter explores the use of silk in biomedical applications and healthcare textiles. Future trends in silk applications are also highlighted.
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Wang, Fei, and Yu-Qing Zhang. "Bioconjugation of Silk Fibroin Nanoparticles with Enzyme and Peptide and Their Characterization." In Advances in Protein Chemistry and Structural Biology, 263–91. Elsevier, 2015. http://dx.doi.org/10.1016/bs.apcsb.2014.11.005.

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"Silks Produced by Insect Labial Glands." In Fibrous Proteins, 120–34. CRC Press, 2008. http://dx.doi.org/10.1201/9781498713689-13.

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"The Elaborate Structure of Spider Silk: Structure and Function of a Natural High Performance Fiber." In Fibrous Proteins, 135–50. CRC Press, 2008. http://dx.doi.org/10.1201/9781498713689-14.

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Griffanti, Gabriele, and Showan N. Nazhat. "Three-Dimensional Bioprinting of Naturally Derived Protein-Based Biopolymers." In Additive Manufacturing in Biomedical Applications, 363–77. ASM International, 2022. http://dx.doi.org/10.31399/asm.hb.v23a.a0006894.

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Abstract This article discusses the state of the art in the 3D bioprinting field. It examines the printability of protein-based biopolymers and provides key printing parameters, along with a brief description of the main current 3D bioprinting approaches. The article presents some studies investigating 3D bioprinting of naturally derived proteins for the production of structurally and functionally biomimetic scaffolds, which create a microenvironment for cells resembling that of the native tissues. It describes key structural proteins processed in the form of hydrogels, such as collagen, silk, fibrin, and others such as elastin, decellularized matrix, and Matrigel (Corning), which are used as biomaterials.
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"Human Uses." In The Chemistry of Plants and Insects: Plants, Bugs, and Molecules, 139–61. The Royal Society of Chemistry, 2017. http://dx.doi.org/10.1039/bk9781782624486-00139.

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Many plant–insect interactions crucially affect human lives, like pollination of crops or insect infestations of useful plants. Some directly benefit our lives. Honey bees produce honey from floral nectars. The composition of honey is discussed. Adulteration of honey can be detected by H-NMR techniques. The chemical composition of beeswax is described and compared with fats and oils and paraffin wax from crude oil. Silk is produced by silk moths whose larvae are raised on a diet of mulberry leaves. Silk, the strongest natural fiber, consists of two main proteins: fibroin and sericin. Several secondary plant metabolites in mulberry leaves make them attractive to silk moth caterpillars. Kermes, a red dye, is derived from the kermes scale insect Kermes vermilio that feeds on kermes oaks. Cochineal is a red dye obtained from the cochineal scale insect (Dactylopius coccus) that lives on cactus pads of the genus Opuntia. Both are anthraquinone dyes. Plant compounds that repel or kill herbivorous insects have diverse chemical structures. Azadirachtin from the neem tree and pyrethrins from the pyrethrum plant are examples of strong insect repellents from plants. Pyrethroids are synthetically derived from pyrethrins. Rotenone from the roots of Derris sp. is a broad-spectrum pesticide. Nicotine is a potent and highly toxic broad-spectrum insecticide. The natural compounds inspired the development of synthetic products.
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Conference papers on the topic "Silk fibroin protein"

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Dogru-Yuksel, Itir Bakis, Chanho Jeong, Byeonghak Park, Mertcan Han, Ju Seung Lee, Tae-il Kim, and Sedat Nizamoglu. "Silk Protein Sheet Origami for Directional Random Biolasers." In Novel Optical Materials and Applications. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/noma.2022.notu3e.2.

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We demonstrate controlled random lasers via origami of dye-doped silk fibroin protein sheets. Folding the films generate nano-scale cracks that form spatially localized feedback and lead to low threshold laser emission.
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Brenckle, M. A., H. Tao, and F. G. Omenetto. "Protein-Protein Imprinting (PPi): High Throughput Nanoscale Imprinting of Silk Fibroin Films for Photonics." In CLEO: Science and Innovations. Washington, D.C.: OSA, 2012. http://dx.doi.org/10.1364/cleo_si.2012.cm4l.2.

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Zhang, Z., H. Jia, Z. Wang, and H. Wu. "Silk Fibroin Protein Coating – An Option for Electrode Gapless Interface to Auditory Neurons." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1686555.

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Qin, Nan, Shaoqing Zhang, and Tiger H. Tao. "Electron regulated 3D nanostructuring of natural silk fibroin protein revealed by near-field nano-spectroscopy." In 2017 19th International Conference on Solid-State Sensors, Actuators and Microsystems (TRANSDUCERS). IEEE, 2017. http://dx.doi.org/10.1109/transducers.2017.7994271.

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Yuruker, Sevket Umut, Mehmet Arik, Enes Tamdogan, Rustamjon Melikov, Sedat Nizamoglu, Daniel Aaron Press, and Ilkem Durak. "Thermal and Optical Performance of Eco-Friendly Silk Fibroin Proteins as a Cavity Encapsulation Over LED Systems." In ASME 2015 International Technical Conference and Exhibition on Packaging and Integration of Electronic and Photonic Microsystems collocated with the ASME 2015 13th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/ipack2015-48326.

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The demand for high power LEDs for illumination applications is increasing. LED package encapsulation is one of most critical materials that affect the optical path of the generated light by LEDs, and may result in lumen degradation. A typical encapsulation material is a mixture of phosphor and a polymer based binder such as silicone. After LED chips are placed at the base of a cavity, phosphor particles are mixed with silicone and carefully placed into the cavity. One of the important technical challenges is to ensure a better thermal conductivity than 0.2 W/m-K of current materials for most of the traditional polymers in SSL applications. In this study, we investigated an unconventional material of the silk fibroin proteins for LED applications, and showed that this biomaterial provides thermal advantages leading to an order of magnitude higher thermal performance than conventional silicones. Silk fibroin is a natural protein and directly extracted from silk cocoons produced by Bombyx mori silkworm. Therefore, it presents a “green” material for photonic applications with its superior properties of biocompatibility and high optical transparency with a minimal absorption. Combining these properties with high thermal performance makes this biomaterial promising for future LED applications. An experimental and computational study to understand the optical and thermal performance is performed. A computational fluid dynamics study with a commercial CFD software was performed and an experimental set-up was developed to validate the computational findings to determine the thermal conductivity of the proposed material.
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Zhang, Shaoqing, Nan Qin, and Tiger H. Tao. "Extracted natural silk fibroin as a dual-tone protein resist for eco-friendly electron beam lithography." In 2017 IEEE 30th International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2017. http://dx.doi.org/10.1109/memsys.2017.7863510.

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Kluge, Jonathan A., Rudra A. Pampati, Mara L. Schenker, Daniel J. Zhou, John E. Esterhai, David L. Kaplan, and Robert L. Mauck. "Delivery of Active FGF-2 From Mechanically-Stable Biological Nanofibers Accelerates Cell Ingress Into Multifiber Composites." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53955.

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Fibrocartilaginous tissues such as the meniscus and annulus fibrosus serve critical load-bearing roles, relying on arrays of highly organized collagen fibers to resist tensile loads [1]. As these specialized structures are often injured, there exists great demand for engineered tissues for repair or replacement. Cell-laden aligned nanofibrous scaffolds formed from poly(ε-caprolactone) (PCL) have shown promise in achieving tissuelike mechanical and biochemical properties and can direct cellular and matrix organization in vitro [2]. A current limitation of nanofibrous scaffolds, however, is a slow rate of cellular infiltration, particularly in thick scaffolds. To address this, dynamic composite nanofibrous scaffolds have been fabricated via multi-fiber spinning [3], which can offer tunable modes of degradation depending on the polymer sources. For example, water-soluble polyethylene oxide (PEO) fibers can be co-spun with PCL to improve porosity and hasten cell ingress [4]. Incorporation of additional tunable and bioactive polymer sources may add greater versatility to these composite systems. For example, aqueous-based silk fibroin can be used as a slow-degrading, mechanically strong composite fiber component [5] into which active biologic factors (drugs, growth factors) can be incorporated [6]. Variably-degradable silk fibers can be formed by modulating post-spinning treatments, and protein release kinetics can likewise be manipulated by the physical crosslinking method [7]. We hypothesized that incorporation of robust and tunable silk protein-based fibers into a composite of slow-degrading synthetic fibers would provide mechanical function while delivering active biologic factors to expedite cell proliferation and encourage more rapid construct colonization. To test this hypothesis, we characterized the release kinetics of recombinant FGF-2 from silk fibers and its bioactivity in vitro and in a rat subcutaneous implant model.
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Buehler, Markus J., and Sebastien Uzel. "Deformation and Failure of Collagenous Tissues: A Multi-Scale Study." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205480.

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Fibrous proteins constitute critical building blocks of life, forming biological materials such as hair, bone, skin, spider silk or cells, which play an important role in providing key mechanical functions in biological systems. However, the fundamental atomistic and molecular deformation and fracture mechanisms of biological protein materials remain largely unknown, partly due to a lack of understanding of how individual protein building blocks respond to mechanical load.
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Manco-Johnson, M. J., T. C. Abshire, and L. J. Jacobson. "FREQUENCY AND IMPLICATIONS OF SEVERE NEONATAL PROTEIN C DEFICIENCY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643609.

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The newborn infant has a physiologically low level of protein C which rises very slowly in postnatal life. The frequency and significance of severe neonatal protein C deficiency has not been reported. In this study, protein C levels were measured in 110 newborn infants at the time of birth using functional (amidolytic, Cact) and immunologic (Laurell rocket, Cag) assays. The protein C levels were compared with a marker of thrombin activation (D-dimer fragment of fibrin, +D-D) and infants were subsequently followed for signs and symptoms of thrombosis. Results are summarized below (protein C levels are expressed as U/ml).Thirteen infants had protein C levels compatible with the homozygous deficiency state. Extremely low levels of protein C (<0.20 U/ml) were not found in well term infants and were rarely noted in stable preterm infants. D-D were infrequently present and no thrombosis occurred. Near term infants born with fetal distress frequently showed +D-D but rarely demonstrated extremely low levels of protein C. None of these infants required indwelling arterial catheters and no thromboses occurred. Preterm infants with severe respiratory distress showed lower protein C levels at birth (p <0.01). Although 71% had +D-D, thromboses in these infants were all related to invasive catheterizations. In contrast, the study population of twins demonstrated a high frequency of severe protein C deficiency with negative D-D and frequent thromboses, three of which occurred in the absence of instrumentation. In summary, severe protein C deficiency and thrombin activation are common in sick preterm infants with the risk of thrombosis increased by intravascular catheterization. In contrast, twins with severe protein C deficiency may manifest a thrombotic risk which is independent of thrombin activation or catheterization.
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