Salt-catalyzed addition reaction of monoepoxides with philosamia cynthia ricini and bombyx mori silk fibroins

The heterogeneous addition reaction of various monoepoxides with silk fibroins of Philosamia cynthia ricini and Bombyx mori was investigated at 45–75°C by use of aqueous solutions of various salts as padding catalysts. The effects of salt on the epoxide–silk fibroin reactions were attributed mainly to the nucleophilicity of the anions and also to the acidity or the electronegativity of the cations. The effect of the substituent of the epoxide on the add-ons was elucidated by the modified Taft equation, (log W ? log W₀)/σ* = ρ_p + ρ_sE_s/σ*, where W₀ and W are the add-ons for the reaction of a given compound and of its substituted derivatives, σ* and E_s are the polar and the steric substituent constants, ρ_p and ρ_s are the polar and the steric reaction constants, respectively. Histidine, lysine, arginine, tyrosine, serine, and acidic amino acids were found to react. The reactivity difference between Philosamia cynthia ricini and Bombyx mori fibroins towards the epoxide was discussed in the light of the observed phenomena.     

Structure and solubility of natural silk fibroin

The solubility of silk fibroin in aqueous-salt, aqueous-organic, and organic media is analyzed. Factors affecting the formation of the secondary structural organization of fibroin in solutions and in the solid state after the recovery from solutions are analyzed.     

Mechanisms of silk fibroin sol-gel transitions

Silk fibroin sol-gel transitions were studied by monitoring the process under various physicochemical conditions with optical spectroscopy at 550 nm. The secondary structural change of the fibroin from a disordered state in solution to a beta-sheet-rich conformation in the gel state was assessed by FTIR and CD over a range of fibroin concentrations, temperatures, and pH values. The structural changes were correlated to the degree of gelation based on changes in optical density at 550 nm. No detectable changes in the protein secondary structure (FTIR, CD) were found up to about 15% gelation (at 550 nm), indicating that these early stages of gelation are not accompanied by the formation of beta-sheets. Above 15%, the fraction of beta-sheet linearly increased with the degree of gelation. A pH dependency of gelation time was found with correlation to the predominant acidic side chains in the silk. Electrostatic interactions were related to the rate of gelation above neutral pH. The overall independencies of processing parameters including concentration, temperature, and pH on gel formation and protein structure can be related to primary sequence-specific features in the molecular organization of the fibroin protein. These findings clarify aspects of the self-assembly of this unique family of proteins as a route to gain control of material properties, as well as for new insight into the design of synthetic silk-biomimetic polymers with predictable solution and assembly properties.     

Simple preparation and characteristics of silk fibroin microsphere

We investigated the biomaterial and pharmaceutical utility of pure silk fibroin (SF) protein as a possible for separation, using Sephadex G-25 gel filtration chromatography and simply preparing SF microsphere particles (SFMP) by spray dryer. Also, some of its physicochemical properties and morphology were investigated. Obtaining microspheres and/or submicronic particles by spray dryer method was accelerated or completed with the transition from the random coil to the β-sheet structure during spray dryer treatment. It was identified by the basic Fourier transform infrared spectroscopy of SFMP. The various pH range of SFMP’s swelling ratio is dependent on the pH of the solution, not on the occurred gelation. Morphologically, SFMP was spherical in shape, and particles, average 2±10 μm in size, were observed by scanning electron microscope and particle analyzer, respectively. The average molecular weight (M_W) of pure SF protein dissolved in calcium chloride is about 61,500 g/mol as measured by gel permeation chromatography.     

Mechanism of the reaction of styrene oxide with phosphonate-carbanions

Assignment of absolute configuration to the trans-2-phenylcyclopropane -carboxylic acid reveals that the reaction between optically active styrene oxide and phosphonate-carbanions proceeds with inversion at the asymmetric centre.     

Gelation behavior of Antheraea pernyi silk fibroin

The sol-gel transition behavior of Antherae pernyi silk fibroin(Ap-SF) has not been systematically investigated.In this work,the influence of environmental temperature,pH,the concentration of Ap-SF,K+ and Ca2+ on the gelation time,and the structural changes of Ap-SF in sol-gel transformation were studied.The results indicated that the gelation time of the Ap-SF aqueous solution decreased with the increase of the Ap-SF concentration and environmental temperature.The sol-gel transformation of Ap-SF was much m...     

气相色谱法同时测定苯乙烯催化氧化反应液中的苯乙烯、环氧苯乙烷和苯甲醛

建立了同时测定苯乙烯催化氧化反应液中的苯乙烯、环氧苯乙烷和苯甲醛的气相色谱分析方法。该法以正庚烷为内标物,在DB-1毛细管色谱柱上进行分离,氢火焰离子化检测器。方法的回收率98%~101.5%,相对标准偏差小于2.0%。     

Physical and chemical properties of tussah silk fibroin films

Physical and chemical structure, as well as thermal behavior of solution-cast regenerated films, prepared from tussah (Antheraea pernyi) silk fibroin, were compared with those of solution-cast native films, in order to ascertain whether treatment (degumming, dissolution) used for preparation affected their properties. Regenerated fibroin films exhibited a higher thermal stability than native ones, as shown by differential scanning calorimetry, thermomechanical analysis, and dynamic mechanical behavior. Glass transition temperature and other relevant thermal transitions of the regenerated silk specimen shifted to higher temperatures compared with those of native specimen. Molecular conformation and crystalline structure did not show significant differences between the two kinds of silk films. Amino acid composition and molecular weight, however, distribution changed markedly after dissolving tussah silk fibroin fiber in concentrated LiSCN in polypeptide size was the main features for the regenerated silk fibroin. © 1994 John Wiley & Sons, Inc.     

Concentration‐dependent conformation transition of regenerated silk fibroin induced by graphene oxide nanosheets incorporation

Regenerated silk fibroin (RSF)/graphene oxide (GO) nanocomposite has been substantially investigated due to its significant multifunctional potential. Here, in combination of micromorphology, crystalline conformation, dynamic mechanical property characterization, and Fourier self‐deconvolution (FSD) quantitative analysis, we investigated the RSF molecular chains conformation transition induced by GO nanosheet incorporation, and its influence on the structural and mechanical properties of solution casted RSF/GO composite films. The GO nanosheet promoted the silk fibroin molecular chains conformation transition from random coil to β‐sheet structure, and a correlation between β‐sheet structure fraction and GO concentration was revealed. The β‐sheet structure fraction increases further improved the dynamic mechanical property of composite films. Moreover, based on nucleation‐dependent aggregation of silk fibroin molecular chains, a mechanism considering the competition effect between GO concentration and its total surface area was proposed to explain the observed concentration‐dependent conformation transition phenomenon. The study improves our understanding on silk fibroin conformation transition process in RSF/GO composite and would provide a valuable reference for the rational design of bioinspired multifunctional materials with enhanced mechanical properties. © 2019 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2019 , 57, 1506–1515     

The influence of UV radiation on silk fibroin

An investigation into the influence of UV-irradiation on regenerated silk fibroin dissolved in water was carried out using UV-Vis and fluorescence spectroscopy. It was found that the absorption of regenerated silk fibroin in solution increased during UV-irradiation of the sample, most notably between 250 and 400 nm. Moreover, after UV-irradiation a wide peak emerged between 290 and 340 nm with maximum at about 305 nm. The new peak suggests that new photoproducts are formed during UV-irradiation of regenerated silk fibroin.The fluorescence of regenerated silk fibroin was observed at 305 nm, at 480 nm and at 601 nm after excitation at 275 nm. UV-irradiation caused fluorescence fading at 305 nm and at 601 nm. The increase of fluorescence was observed at 480 nm, probably due to formation of new photoproducts. After excitation at 305 nm the fluorescence of regenerated silk fibroin was observed at 340 nm and at 400 nm. UV-irradiation caused fluorescence fading at 340 nm. FTIR spectroscopy showed that primary structure of regenerated silk fibroin was not significantly affected by UV radiation. SDS-PAGE chromatography showed alterations of molecular weight of silk after UV exposure.     

Biomaterial coatings by stepwise deposition of silk fibroin

A completely aqueous, stepwise deposition process with Bombyx mori silk fibroin for the assembly of nanoscale thin film coatings is reported the first time. The focus of this work was to develop an understanding of the control of this deposition process and to characterize the films formed from a physicochemical perspective. The deposition process was monitored by UV spectrophotometry and research quartz crystal microbalance. Both absorbance and film thickness correlated linearly with the number of silk fibroin layers deposited, analogous to multilayered materials fabricated from conventional polyelectrolytes. The polymer adsorption process was stable and reproducible, with control of a single layer thickness ranging from a few to tens of nanometers, determined by the concentrations of silk fibroin, salt concentration in the dipping solution, and method of rinsing. The driving force for the assembly of silk fibroin onto the substrate was primarily hydrophobic interactions, while some electrostatic interactions were also involved. The difference with this approach from traditional polyelectrolyte layer-by-layer techniques is that an intervening drying step is used to control the structure and stability of the self-assembled silk fibroin. The assembled films were stable under physiological conditions and supported human bone marrow stem cell adhesion, growth, and differentiation. This approach offers new options to engineer biomaterial coatings as well as bulk materials with control of both interfacial properties conducive to specific cellular or tissue responses and the potential to entrap and deliver labile molecules or other components due to the all-aqueous process described.     

Preparation and characterization of conjugates of silk fibroin and chitooligosaccharides

With the aim of the functionalization of silk fibroin (SF), conjugates of SF and polycationic chitooligosaccharides (COS) were prepared by the chemical modification of SF with cyanuric chloride (CY)-activated COS (COS-CY). The ¹H NMR spectrum of the reaction product between a model compound D-glucosamine and CY suggested that the COS-CY modifier was synthesized by the reaction of the amino group and the terminal anomeric hydroxyl group in COS, with the chlorine atom of CY. The ¹H NMR spectrum and amino acid analysis of the conjugates (COS-CY-SF) clarified that the tyrosine and lysine residues of SF reacted with a second chlorine atom of the triazine ring of the modifier. On the basis of the results of the hexosamine determination and the amino acid analysis of COS-CY-SF, it is estimated that COS-CY-SF consists of 38 wt% COS, 8 wt% CY, and 54 wt% SF. The absorbance at 600 nm as a function of pH for COS-CY-SF and SF indicated that the introduction of a large amount of hexosamine made SF amphiphilic and more water-soluble at lower pH values. The COS-CY-SF conjugates retarded the growth of Escherichia coli after incubation for 24 h at a conjugate concentration of 0.6% (w/v), while SF did not retard the growth at a SF concentration of 0.7% (w/v).     

Preparation and characterization of chitin whisker-reinforced silk fibroin nanocomposite sponges

For highly porous form such as sponges or scaffolds, the induction of the β-sheet formation of silk fibroin to make the water-stable materials usually results in their high shrinkage leading to a difficulty in controlling shape and size of materials. Thus, the objective of this study was to improve dimensional stability of silk fibroin sponge by incorporating chitin whiskers as nanofiller. Chitin whiskers exhibited the average length and width of 427 and 43 nm, respectively. Nanocomposite sponges at chitin whiskers to silk fibroin weight ratio (C/S ratio) of 0, 1/8, 2/8, or 4/8 were prepared by using a freeze-drying technique. The dispersion of chitin whiskers embedded in the silk fibroin matrix was found to be homogeneous. The presence of chitin whiskers embedded into silk fibroin sponge not only improved its dimensional stability but also enhanced its compression strength. Regardless of the chitin whisker content, SEM micrographs showed that all samples possessed an interconnected pore network with an average pore size of 150 μm. To investigate the feasibility of the nanocomposites for tissue engineering applications, L929 cells were seeded onto their surfaces, the results indicated that silk fibroin sponges both with and without chitin whiskers were cytocompatible. Moreover, when compared to the neat silk fibroin sponge, the incorporation of chitin whiskers into the silk fibroin matrix was found to promote cell spreading.     

Separation of thorium from aqueous solution using silk fibroin

In this study we investigate the basic features of thorium adsorption from aqueous systems by silk fibroin. Our previous study showed that this biopolymer has high efficiency for U(VI) adsorption. It is well-known that thorium, which is a tetravalent metal, is a more reactive element than uranium. Thorium(IV) adsorption proves to be very rapid and dependent on pH, temperature, retention time, concentration of ion, amount of fibroin, volume of solution and volume-to-mass ratio.     

Effects of poloxamer on the gelation of silk fibroin

The influence of the concentration of poloxamer 407, the pH and the temperature on the gelation of silk fibroin (SF) were studied. It was found that the gelation of SF occurred in the presence of poloxamer at pH value of 7.0 while gelation of SF itself did not occur. The gelation time of SF was shortened with increasing the poloxamer concentration and the temperature. The sol‐gel transition of SF became reversible with an addition of poloxamer. From infrared (IR) and circular‐dichroism (CD) spectroscopy measurements, it was found that a conformational change of the SF in the SF/poloxamer system from random coil to β‐structure was accelerated after forming a polymer complex with the poloxamer. The crystallinity of the poloxamer was reduced by SF from X‐ray diffraction measurements.     

Proteomic profiling of the photo-oxidation of silk fibroin: implications for historic tin-weighted silk

The stability of silk proteins to ultraviolet light is an issue of significant concern in both the appearance retention of silk-derived products and the preservation of historic silk textiles. Until now, evaluation of silk degradation has only been performed at the holistic, rather than molecular level. This article describes the first proteomic profiling of silk photo-oxidation, characterizing protein primary level modification leading to coloration changes, and evaluating the effects of tin weighting on photodegradation. Heavy-chain fibroin, the main proteinaceous component of the silk thread, is a repetitive, highly crystalline protein with a content rich in tyrosine. Photoproducts of tyrosine were characterized and the levels of oxidative modification at the protein primary structural level correlated with changes in coloration and tensile strength. The effect of tin as a weighting agent used on historical fabrics was examined. Tin-weighted fabrics were evaluated following two treatments (pink and dynamite) and proteomic analysis revealed a significant increase in oxidatively modified amino acid residues within the pink-treated silk. These findings offer new insight into the molecular-level oxidation of silk proteins under UV exposure, and the effects of silk treatments in either exacerbating or ameliorating this degradation.