• International Journal of Industrial Entomology and Biomaterials
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• v.31 no.1
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• pp.1-6
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• 2015

Recently, sericin has attracted increasing attention in biomedical and cosmetic research because of its useful properties including acceleration of wound healing, improvement of cell attachment, and inhibition of ultraviolet-B induced apoptosis. However, sericin films have poor mechanical properties, which restricts the application to those fields. In this study, cellulose nanofibril (CNF)/sericin composite films were fabricated by solvent casting, and the effects of ultrasonication time and CNF content on the solution turbidity, molecular conformation, and film mechanical properties of sericin film were examined. As the ultrasonication time increased, the turbidity of the CNF/sericin suspension decreased. Conversely, as the CNF content increased, the turbidity increased. However, ${\beta}$-sheet crystallization and mechanical properties remained almost unchanged by varying the ultrasonication time and CNF content, indicating that CNF is not effective to improve the mechanical properties of sericin films.

• Archives of Pharmacal Research
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• v.15 no.1
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• pp.52-57
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• 1992

The molecular structure of a natural compound was determined by single crystal X-ray diffraction analysis. The compound was isolated by methanol extraction and repeated chromatography from the stem of Paulownia tomentosa. Yellow prismatic crystals of the compound, which were recrystallized from tetrahydrofuran, are triclinic, with a = 7.310 (6), b = 10.753(6), c = 11.586(5) ${\AA}.\;\alpha= 93.30(6),\;\beta=105.62(10),\;\gamma=109.49(7)^\circ,\;D_x=1.514,\;D_m=1.51 g/cm^3$, space group P1 and Z = 2. The structure was solved by direct method, and refined by least-squares procedure to the final R-value of 0.032 for 1271 independent reflections $(F\le3\sigma{(F))}$. The compound is one of new furanquinone analogue. The molecule has a nearly planar conformation with an intramolecular hydrogen bond. In the crystal, the planar molecules are arranged as a prallel sheet-like pattern, and these stackings are stabilized by the O-H...O type intermolecular hydrogen bonds. The other intermolecular contacts appear to be the normal van der Waals interactions.

• BMB Reports
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• v.35 no.3
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• pp.343-347
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• 2002

The human protein tyrosine kinase-6 (PTK6) polypeptide that is deduced from the cDNA sequence contains a Src homology (SH) 3 domain, SH2 domain, and catalytic domain of tyrosine kinase. We initiated biochemical and NMR characterization of PTK6 SH3 domain in order to correlate the structural role of the PTK6 using circular dichroism and heteronuclear NMR techniques. The circular dichroism data suggested that the secondary structural elements of the SH3 domain are mainly composed of $\beta$-sheet conformations. It is most stable when the pH is neutral based on the pH titration data. In addition, a number of cross peaks at the low-field area of the proton chemical shift of the NMR spectra indicated that the PTK6 SH3 domain retains a unique and folded conformation at the neutral pH condition. For other pH conditions, the SH3 domain became unstable and aggregated during NMR measurements, indicating that the structural stability is very sensitive to pH environments. Both the NMR and circular dichroism data indicate that the PTK6 SH3 domain experiences a conformational instability, even in an aqueous solution.

• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.2
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• pp.175-179
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• 2010

Silk fibroin membrane was prepared and examined to know the feasibility of SF membrane as guided bone regeneration. The morphology of silk membrane was flat and smooth surface. The conformation of silk fibroin was $\beta$-sheet structure. When the silk membrane was applied on the rat calvarial defect model, it showed significantly higher new bone formation than uncovered control in histomorphometric analysis. The silk membrane was covered by thin fibrotic tissue and there was not observed any inflammatory cells infiltration. In conclusion, silk fibroin membrane could be useful materials for guided bone regeneration.

• International Journal of Industrial Entomology and Biomaterials
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• v.28 no.2
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• pp.66-70
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• 2014

In order to the feasibility of silk materials as protein delivery system, silk beads incorporated with bovine serum albumin (BSA) were prepared by dropping silk fibroin extract into dope solution composed of ethanol and dichloromethane. Structural and morphological characteristics of silk beads were examined using scanning electron microscopy (SEM), infrared spectrometry, and X-ray diffractometry. Swelling ratio of silk beads was also measured. Release behavior of prototypical protein, BSA, was studied by observing the electropheretic phenomenon and release profile. SEM showed that silk beads are spherical with porous interior structure. Infrared spectrometry and X-ray diffraction confirm that the silk beads have a ${\beta}$-sheet conformation. The swelling capability of silk beads increased with the incorporation of the protein. The protein was released from the beads with slow release following an initial burst release. Therefore, silk beads show promise as materials for encasing protein drugs to be delivered to targets in the human body.

• BMB Reports
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• v.35 no.2
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• pp.143-154
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• 2002

The structural and functional aspects of ervatamin B were studied in solution. Ervatamin B belongs to the $\alpha+\beta$ class of proteins. The intrinsic fluorescence emission maximum of the enzyme was at 350 nm under neutral conditions, and at 355 nm under denaturing conditions. Between pH 1.0-2.5 the enzyme exists in a partially unfolded state with minimum or no tertiary structure, and no proteolytic activity. At still lower pH, the enzyme regains substantial secondary structure, which is predominantly $\beta$-sheet conformation and shows a strong binding to 8-anilino-1-napthalene-sulfonic acid (ANS). In the presence of salt, the enzyme attains a similar state directly from the native state. Under neutral conditions, the enzyme was stable in urea, while the guanidine hydrochloride (GuHCl) induced equilibrium unfolding was cooperative. The GuHCl induced unfolding transition curves at pH 3.0 and 4.0 were non-coincidental, indicating the presence of intermediates in the unfolding pathway. This was substantiated by strong ANS binding that was observed at low concentrations of GuHCl at both pH 3.0 and 4.0. The urea induced transition curves at pH 3.0 were, however, coincidental, but non-cooperative. This indicates that the different structural units of the enzyme unfold in steps through intermediates. This observation is further supported by two emission maxima in ANS binding assay during urea denaturation. Hence, denaturant induced equilibrium unfolding pathway of ervatamin B, which differs from the acid induced unfolding pathway, is not a simple two-state transition but involves intermediates which probably accumulate at different stages of protein folding and hence adds a new dimension to the unfolding pathway of plant proteases of the papain superfamily.

• Molecules and Cells
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• v.27 no.6
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• pp.673-680
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• 2009

Conversion of the normal soluble form of prion protein, PrP ($PrP^C$), to proteinase K-resistant form ($PrP^{Sc}$) is a common molecular etiology of prion diseases. Proteinase K-resistance is attributed to a drastic conformational change from ${\alpha}$-helix to ${\beta}$-sheet and subsequent fibril formation. Compelling evidence suggests that membranes play a role in the conformational conversion of PrP. However, biophysical mechanisms underlying the conformational changes of PrP and membrane binding are still elusive. Recently, we demonstrated that the putative transmembrane domain (TMD; residues 111-135) of Syrian hamster PrP penetrates into the membrane upon the reduction of the conserved disulfide bond of PrP. To understand the mechanism underlying the membrane insertion of the TMD, here we explored changes in conformation and membrane binding abilities of PrP using wild type and cysteine-free mutant. We show that the reduction of the disulfide bond of PrP removes motional restriction of the TMD, which might, in turn, expose the TMD into solvent. The released TMD then penetrates into the membrane. We suggest that the disulfide bond regulates the membrane binding mode of PrP by controlling the motional freedom of the TMD.

• International Journal of Industrial Entomology and Biomaterials
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• v.37 no.2
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• pp.36-42
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• 2018

Recently, silk sericin has attracted attention because of its unique properties as a biomaterial, including its UV resistance, moisturizing effect on skin, and wound-healing effect. Therefore, the preparation of sericin in various forms such as gel, film, fiber, and sponge is studied for cosmetic and biomedical applications, and the effect of the preparation conditions on the structure and properties of sericin forms is examined to maximize its performance. In this study, silk sericin films were prepared under different preparation conditions and heat-treated at high temperatures ($100-250^{\circ}C$) to examine the effect of heat treatment on the film structure. The order of the crystallinity index of the untreated sericin film is as follows: F25 (sericin film cast from formic acid) > WE25 (ethanol treated sericin film cast from water at $250^{\circ}C$) > W25 (sericin film cast from water at $250^{\circ}C$) > W100 (sericin film cast from water at $100^{\circ}C$). As the heat-treatment temperature was increased, the color of the sericin films changed gradually from colorless to yellow, brown, and black depending on the temperature. The crystallinity of the sericin film changed after the heat treatment, depending on the preparation condition. Whereas a sericin film cast from formic acid (F25) started to lose its crystallinity at $200^{\circ}C$, thus undergoing the highest loss of crystallinity among the sericin films studied, the rest (W25, WE25, and W100) showed a decrease in crystallinity at $250^{\circ}C$, owing to the disruption of the ${\beta}$-sheet crystallites due to heat.

• Food Science and Biotechnology
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• v.18 no.1
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• pp.228-233
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• 2009

This study was conducted to examine the changes in the molecular structure and physiological activities of silk fibroin by gamma irradiation. The results of gel permeation chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the molecular weight of fibroin was increased depending upon the irradiation dose. Secondary structure of fibroin determined by using circular dichroism revealed that the ratio of $\alpha$-helix was increased up to 10 kGy and then decreased depending upon the irradiation dose. Whereas, the ratio of $\beta$-sheet, $\beta$-turn, and random coil were decreased and then increased with an alteration in the $\alpha$-helix secondary conformation. The 2.2-diphenyl-1-picryl-hydrazil (DPPH) radical scavenging activity of fibroin was increased by gamma irradiation at 5 kGy, but was decreased above 10 kGy depending upon the irradiation dose. Also, the inhibition activities of tyrosinase and melanin synthesis of fibroin were increased by gamma irradiation. These results indicated that gamma irradiation could be used as an efficient method to make fibroin more suitable for the development of functional foods and cosmetics.