• International Journal of Industrial Entomology and Biomaterials
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• v.38 no.2
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• pp.51-55
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• 2019

The structure and properties of silk polymers (fibroin and sericin) can be satisfactorily controlled by choosing a suitable silkworm variety and, hence, this parameter (i.e., silkworm variety) has attracted increasing attention. A previous study reported that the crystallinity of white colored silkworm cocoons depends on the silkworm variety. In the present study, sixteen yellow colored silkworm variety cocoons were produced and their molecular conformation and crystallinity were investigated. The conformation of the silkworm cocoons varied with the silkworm variety. Most cocoons exhibited ${\beta}$-sheet conformation, although random coil and ${\beta}$-sheet conformations co-existed in some cocoons (e.g., 21 and D90). The crystallinity of the silkworm cocoons varied with the silkworm variety and the measurement position of the cocoon (i.e., outer surface or inner surface). However, the difference in the crystallinity indices of the outer and inner surfaces comprising the cocoons varied with the silkworm variety, but was <2% for all cocoons, except for MAL.

• International Journal of Industrial Entomology and Biomaterials
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• v.33 no.2
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• pp.144-148
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• 2016

Recently, silk sericin has been studied extensively for biomedical and cosmetic applications because of its unique properties, including UV resistance and wound healing ability. For use in applications, sericin is fabricated in various forms including films and gels. However, the mechanical properties of sericin are too weak. In this basic study on improving the mechanical properties of sericin, a silk sericin aqueous solution was separated into two layers by centrifugation. The solution viscosity, molecular conformation, and mechanical properties of each separation layer of the sericin were examined. Sericin from the lower layer had a higher solution viscosity and film mechanical properties (strength and strain) than that from the upper layer, implying that sericin from the lower layer had a higher molecular weight than that from the upper layer. The molecular conformation of the sericin films varied depending on the casting solvent. In aqueous solution, the sericin film from the lower layer showed a ${\beta}$-sheet conformation, whereas that from the upper layer displayed a random coil conformation. All the sericin films showed a highly ${\beta}$-sheet-crystallized state when cast in formic acid, regardless of the separation layer.

• Journal of Sericultural and Entomological Science
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• v.42 no.1
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• pp.42-47
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• 2000

Structural and thermal characteristics of silk fibroin/poly(2-hydroxyethyl methacrylate)(PHEMA) blend films were investigated using FTIR, X-ray diffractometer, differential scanning calorimeter, thermogravimeter and scanning electron microscope. FTIR spectra showed that the conformation of silk fibroin prepared by dissolving in formic acid was $\beta$-sheet, which did not affected by blending with PHEMA. The X-ray diffraction patterns also showed that individual crystalline structure of silk fibroin and PHEMA was not affected for the blend films. The initial thermal decomposition temperature of silk fibroin/PHEMA blend film tends to be higher than either of silk fkbroin or PHEMA. Thermal stability of both polymers, more notably PHEMA, can be improved by blending two components. As a result of SEM observation, the phases separation for silk fibroin/PHEMA blend films occured regardless of blend ratio ; continuous and dispersed phase were silk fibroin and PHEMA component, respectively.

• Bulletin of the Korean Chemical Society
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• v.25 no.6
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• pp.838-842
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• 2004

Amyloid peptide (A${\beta}$) is the major component of senile plaques found in the brain of patient of Alzheimer's disease. ${\beta}$-amyloid peptide (25-35) (A${\beta}$25-35) is biologically active fragment of A${\beta}$. The three-dimensional structure of A${\beta}$25-35 in aqueous solution with 50% (vol/vol) TFE determined by NMR spectroscopy previously adopts an ${\alpha}$-helical conformation from $Ala^{30}$ to $Met^{35}$. It has been proposed that A${\beta}$(25-35) exhibits pH- and concentration-dependent ${\alpha}-helix{\leftrightarrow}{\beta}$sheet transition. This conformational transition with concomitant peptide aggregation is a possible mechanism of plaque formation. Here, in order to gain more insight into the mechanism of ${\alpha}$-helix formation of A${\beta}$25-35 peptide by TFE, which particularly stabilizes ${\alpha}$-helical conformation, we studied the secondary-structural elements of A${\beta}$25-35 peptide by molecular dynamics simulations. Secondary structural elements determined from NMR spectroscopy in aqueous TFE solution are preserved during the MD simulation. TFE/water mixed solvent has reduced capacity for forming hydrogen bond to the peptide compared to pure water solvent. TFE allows A${\beta}$25-35 to form bifurcated hydrogen bonds to TFE as well as to residues in peptide itself. MD simulation in this study supports the notion that TFE can act as an ${\alpha}$-helical structure forming solvent.

• International Journal of Industrial Entomology and Biomaterials
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• v.26 no.2
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• pp.113-118
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• 2013

In this study, silk sericin films were prepared using different extraction methods, and the molecular conformation of sericin was examined using Fourier-transform infrared spectroscopy with attenuated total reflection geometry. Additionally, the effect of the film side (air-facing side or plate-facing side) on the molecular conformation of the sericin films was investigated. Interestingly, the molecular conformation of the sericin film depended on the film side. The molecular conformation of air-facing side of the sericin film was significantly influenced by extraction solution and time. The ${\beta}$-sheet crystallization and the crystallinity index of the sericin film markedly increased with an increase in the extraction time in hot water. The order of the crystallinity indices for the sericin films obtained with different extraction solutions was as follows: citric acid solution > urea solution >> hot water. In contrast, no remarkable differences were observed in the molecular conformation of the plate-facing side of the sericin film after extraction in hot water for different time periods. Urea and citric acid solution extractions showed remarkably higher crystallinity indices for sericin than those obtained after hot water extraction. However, no significant differences were observed in the crystallinity index of sericin between urea and citric acid solution extraction in plate-facing side of the film.

• Journal of Sericultural and Entomological Science
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• v.41 no.1
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• pp.54-60
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• 1999

Antheraea pernyi silk powder was prepared by treatment with HCl and NaOH. The degree of hydrolysis of Antheraea pernyi silk fiber was examined. The morphology and structural characteristics of Antheraea pernyi silk powder were investigated by using SEM, FTIR and X-ray diffractometer. As the concentration of HCl and NaOH and tratment temperature increased, in general, the degree of hydrolysis of Antheraea pernyi silk fiber increased. On the other hand, the degree of hydrolysis of Antheraea pernyi treated with 3 N NaOH at 120$^{\circ}C$ for 24 hr was 70 wt%, which was lower than that of 90$^{\circ}C$(83 wt%). The morphology of acid/alkali resistance fraction of Antheraea pernyi silk fibroin was transformed from fiber form to powered one with an increase of hydrolysis. The conformation of Antheraea pernyi silk powder characterized by FT-IR spectrometer and X-ray diffractometer ${\beta}$-sheet and ${\alpha}$-helix structure.

• Journal of Sericultural and Entomological Science
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• v.44 no.2
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• pp.87-92
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• 2002

Dissolution of Antheraea pernyi silk fiber was carried out in a zinc chloride solution with various dissolving conditions. The solubility was significantly dependent on the concentration of zinc chloride, dissolving temperature and time. The proper conditions of dissolution were found as 8 M zinc chloride, 70$^{\circ}C$ temperature and 30 min dissolving time. Regenerated A. pernyi silk fibroin powder was obtained through dialysis. FTIR and XRD showed that regenerated A. pernyi silk powder was composed of a ${\beta}$-sheet as well as an ${\alpha}$-helix conformation.

• Journal of Sericultural and Entomological Science
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• v.53 no.2
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• pp.118-123
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• 2015

The structural transition of silk protein has been induced by various method including alcohol treatment. To know the effect of alcohol concentration on silk beads conformation, silk beads were prepared in different alcohol concentration (100%, 70%, and 50%) and then examined the infrared spectra of silk beads. Silk beads prepared in 100% alcohol showed at $1265cm^{-1}$ attributed ${\beta}-sheet$ conformation and did not showed a characteristic absorption peak from model drug. However, silk beads in 70% and 50% alcohol showed some peaks originated from model drug including $2933cm^{-1}$, $1069cm^{-1}$, and $973cm^{-1}$. These results means that the micro-environment of silk beads was affected by alcohol concentration.

• Journal of Sericultural and Entomological Science
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• v.52 no.1
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• pp.10-15
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• 2014

Regenerated Antheraea pernyi silk sponge was prepared using calcium nitrate 4 hydrate melt and examined the conformational changes treated with aqueous ethanol solution. The conformation of silk sponges was changed from random coil structure to ${\beta}$-sheet and ${\alpha}$-helix conformation with low ethanol concentration (50 ~ 70%). On the other hand, that of silk sponges with 80% ethanol treatment showed ${\beta}$-sheet ($700cm^{-1}$), ${\alpha}$-helix ($625cm^{-1}$), and random coil ($660cm^{-1}$) specific peaks. Wound healing effect in vitro was observed by cytoslective wound healing kit. Therefore, regenerated Antheraea pernyi silk sponges might be used as promising wound dressing materials.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.149-153
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• 2001

To investigate the mode of bactericidal action for antimicrobial peptide, pediocin, synthetic and mutant pediocins were prepared by direct chemical synthesis. Native pediocin was purified from Pedio-coccus acidilactici M and its conformational structure and bactericidal functions were analyzed and compared to synthetic pediocin. Schematic mode of pediocin actions, how pediocin binds on the target cell membrane, penetrates and makes tunnel are proposed. For these purposes, primary and secondary structures of pediocin was analyzed and disulfide bond assignment was also done. The pediocin purified from P. acidilactici M had high effective bactericidal ability against gram positive bacteria, especially Listeria monocytogenes and was very stable at extreme pHs and even at high temperatures such as autoclaving temperature (121$^{\circ}C$). Pediocin was consisted of 44 amino acids with four cysteines. Novel synthetic peptides were achieved by solid phase peptide synthesis(SPPS) method. To explain the function of cysteine in C-terminal region, mutant pediocin, Ped[C24A＋C44A], was synthesized and their structural and biological functions were analyzed. Second mutant pediocin, Ped[KllE], was prepared to explain the function of lysine at 11 of N-terminal part of pediocin, especially loop of $\beta$-sheet, and to predict the initial binding site of pediocin. The native and synthetic pediocins was showed random coil conformation by spectropolarimetry in moderate conditions. This conformation was observed in extreme conditions such as high temperature and low and high pHs, also. Circular dichroism(CD) data also showed the existence of $\beta$-turn structure in N-terminal part both native and synthetic pediocins. A structural model for pediocin predicts that 18 amino acids in the N-terminal part of the peptide assume a three-strand $\beta$-sheet conformation. This random coil in C-terminal part of pediocin was converted to folding structure, helix structure, in nonpolar solvents such as alcohol and TFE. The disulfide bond between $^{9}$ Cys and $^{14}$ Cys was concrete and inevitable, however, evidences of disulfide bond between $^{24}$ Cys and $^{44}$ Cys was not. Data of Ped[C24A＋C44A], pediocin mutant showed that $^{44}$ Cys was required during killing the target cells but not inevitable, since Ped[C24A＋C44A] still have bactericidal activity but much less than native pediocin. Another pediocin mutant, Ped[KllE], had still bactericidal activity, was controversial to propose that positive charge like as $^{11}$ Lys in loop or hinge in bacteriocin bound or helped to binding to microorganism with electrostatic interaction between cell membrane especially teichoic acid and positive amino acid nonspecifically. The conformation of pediocin among native, synthetic and mutant pediocins did not show big difference. The conformations between oxidized and reduced pediocin were almost similar regardless of native or synthetic.