• Macromolecular Research
• /
• v.16 no.6
• /
• pp.539-543
• /
• 2008

Many natural proteins self-assemble in complex ways, either to fulfill their biological function or introduce particular properties, such as high strength and toughness. We report the morphological transition in water from a spherical to rod-like shape of Bombyx mori silk fibroin by reducing the pH. Transmission electron microscopy, scanning electron microscopy, and dynamic light scattering were used to characterize the dilute solutions of silk fibroin in an aqueous environment, and provide direct visualization of the transformation of spherical micelles at pH 6.8 to nanofibrils at pH 4.8. This change in morphology occurred as a result of the stretching entropy due to the formation of $\beta$-sheets, which was analyzed using circular dichroism spectroscopy. This study demonstrates the self-assembly of silk fibroin as a function of pH.

• Proceedings of the Korean Vacuum Society Conference
• /
• 2010.02a
• /
• pp.377-377
• /
• 2010

FINEMET type nanocrystalline materials synthesized by controlled crystallization of amorphous ribbons[1] exhibit excellent soft magnetic properties making them attractive for technological applications. Present work reports the electronic structure studies of Co-substituted FINEMET to get information on the effect of successive Co substitution on local environment around Fe and Co atom by using near edge x-ray absorption fine structure (NEXAFS) and x-ray magnetic circular dichroism (XMCD) measurements. NEXAFS spectroscopy and XMCD measurements have been carried out at Fe $L_{3,2}$ and Co $L_{3,2}$-edges to investigate the chemical states and electronic structure of FINEMET [$(Fe_{100-x}Co_x)_{78}Si_9Nb_3Cu_1Ba$](0$L_{3,2}$-edge reveal that Fe is in 2+ state and in tetrahedral symmetry with other elements. The magnetic properties exhibiting soft magnetic behavior[2] are discussed on the basis of the electronic structure studied through XMCD.

• Food Science and Biotechnology
• /
• v.15 no.3
• /
• pp.418-423
• /
• 2006

Egg white powders (EWPs) were produced after pH adjustment (PH 6-9) of fresh egg white, followed by spray-drying, and foaming and gelling properties of EWPs were examined. EWP produced after pH adjustment to 6.5 (EWP-6.5) resulted in significantly higher foaming ability and gel hardness than control and other pH-adjusted EWP. Significant increases in surface -SH content and surface hydrophobicity of EWP-6.5 coincided with improved foaming ability and gel hardness. Significantly higher consistency index for reconstituted EWP-6.5 indicates unfolding of egg white protein was substantially increased in EWP-6.5. Decreased a-helix content in EWP-6.5 was confirmed by circular dichroism spectral analysis. These results indicate pH adjustment prior to spray-drying leads to structural changes in egg white proteins, significantly affecting major functionalities of EWP.

• Journal of Applied Biological Chemistry
• /
• v.64 no.4
• /
• pp.391-397
• /
• 2021

Four compounds were isolated from Salvia plebeia aerial parts. Silica gel open column chromatography with a gradient elution system was used to isolate and purify these compounds. Nuclear magnetic resonance spectroscopy and mass spectroscopy were used for structural elucidation and identification, while electronic circular dichroism was used to confirm the absolute configuration. The structures were determined to be 𝛽-sitosterol (1), (-)-1S,5S,8S,10R-1-acetoxy-8-hydroxy-2-oxoeudesman-3,7(11)-dien-8,12-olide (2), ursolic acid (3), and N-methylhydroxylamine (4). Compounds 2 and 4 were isolated for the first time from this plant. Compound 2 was quantitatively analyzed via HPLC/UV. The results showed that the methanol extract of S. plebeia had a higher content of compound 2 (1.20 mg/g) than the ethanol extract (0.55 mg/g). This study could be used as a preliminary step in conducting HPLC/UV analysis of sesquiterpenoids in S. plebeia extract to assess their bioavailability and potency.

• International Journal of Industrial Entomology and Biomaterials
• /
• v.42 no.2
• /
• pp.25-32
• /
• 2021

Mulberry fruit (Morus alba L.) contains phytochemicals, including 1-deoxynojirimycin, quercetin-glucoside, kaempferol-glucoside, and anthocyanins, which have antioxidant effects. In this study, mulberry fruit extract was prepared at various temperatures (25-100℃) and water/ethanol solvent concentrations (0%-100% ethanol). Fourier-transform infrared spectroscopy (FT-IR) and circular dichroism (CD) data indicated that the content of bioactive compounds such as polyphenols and flavonoids was lower in 100% ethanolic extracts than in 30%-50% ethanolic extracts. Radical scavenging activity determined using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-di-3-ethylbenzthiazoline sulfonic acid (ABTS) assays was highly correlated with polyphenol and flavonoid content. In conclusion, 30%-50% ethanolic extracts contained the highest contents of bioactive compounds and exhibited high levels of radical scavenging activity. These findings may inform the use of mulberry fruit extract as a functional food.

• Current Applied Physics
• /
• v.18 no.11
• /
• pp.1190-1195
• /
• 2018

By employing soft X-ray magnetic circular dichroism (XMCD), soft X-ray absorption spectroscopy (XAS), and photoemission spectroscopy (PES), we have investigated the electronic structure of the candidate zero-moment half-metallic $Mn_3Ga$. We have studied the ball-milled and annealed $Mn_3Ga$ powder samples that exhibit nearly zero magnetization. Mn 2p XAS revealed that Mn ions in $Mn_3Ga$ are nearly divalent for both of the Mn ions having the locally octahedral symmetry and those having the locally tetrahedral symmetry. The measured Mn 2p XMCD spectrum of $Mn_3Ga$ is very similar to that of ferrimagnetic $MnFe_2O_4$ having divalent Mn ions. The sum-rule analysis of the Mn 2p XMCD spectrum shows that both the spin and orbital magnetic moments of Mn ions in $Mn_3Ga$ are negligibly small, in agreement with the nearly compensated-ferrimagnetic ground state of $Mn_3Ga$. The valence-band PES spectrum of $Mn_3Ga$ agrees well with the calculated density of states, supporting the half-metallic electronic structure of $Mn_3Ga$.

• Journal of Microbiology and Biotechnology
• /
• v.30 no.12
• /
• pp.1810-1818
• /
• 2020

Inhibitor K562 (IK) protein was first isolated from the culture medium of K562 cells, a leukemia cell line, and is an inhibitory regulator of interferon-γ-induced major histocompatibility complex class II expression. Recently, exogenous truncated IK (tIK) protein showed potential as a therapeutic agent for inflammation-related diseases. In this study, we designed a novel putative anti-inflammatory peptide derived from tIK protein based on homology modeling of the human interleukin-10 (hIL-10) structure, and investigated whether the peptide exerted inhibitory effects against pro-inflammatory cytokines such as IL-17 and tumor necrosis factor-α (TNF-α). The peptide contains key residues involved in binding hIL-10 to the IL-10 receptor, and exerted strong inhibitory effects on IL-17 (43.8%) and TNF-α (50.7%). In addition, we used circular dichroism spectroscopy to confirm that the peptide is usually present in a random coil configuration in aqueous solution. In terms of toxicity, the peptide was found to be biologically safe. The mechanisms by which the short peptide derived from human tIK protein exerts inhibitory effects against IL-17 and TNF-α should be explored further. We also evaluated the feasibility of using this novel peptide in skincare products.

• Bulletin of the Korean Chemical Society
• /
• v.34 no.7
• /
• pp.2117-2124
• /
• 2013

The binding properties and sequence selectivities of ${\Delta}{\Delta}$- and ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ (bip = 4,4'-biphenylene (imidazo [4,4-f][1,10]phenanthroline) complexes with $poly[d(A-T)_2]$ and $poly[d(G-C)_2]$ were investigated using conventional spectroscopic methods. When bound to $poly[d(A-T)_2]$, a large positive circular dichroism (CD) spectrum was induced in absorption region of the bridging moiety for both the ${\Delta}{\Delta}$- and ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complexes, which suggested that the bridging moiety sits in the minor groove of the polynucleotide. As luminescence intensity increased, decay times became longer and complexes were well-protected from the negatively charged iodide quencher compared to that in the absence of $poly[d(A-T)_2]$. These luminescence measurements indicated that Ru(II) enantiomers were in a less polar environment compared to that in water and supported by minor groove binding. An angle of $45^{\circ}$ between the molecular plane of the bridging moiety of the ${\Delta}{\Delta}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complex and the local DNA helix axis calculated from reduced linear dichroism ($LD^r$) spectrum further supported the minor groove binding mode. In the case of ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complex, this angle was $55^{\circ}$, suggesting a tilt of DNA stem near the binding site and bridging moiety sit in the minor groove of the $poly[d(A-T)_2]$. In contrast, neither ${\Delta}{\Delta}$-nor ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complex produced significant CD or $LD^r$ signal in the absorption region of the bridging moiety. Luminescence measurements revealed that both the ${\Delta}{\Delta}$- and ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complexes were partially accessible to the $I^-$ quencher. Furthermore, decay times became shorter when bis-Ru(II) complexes bound to $poly[d(G-C)_2]$. These observations suggest that both the ${\Delta}{\Delta}$- and ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ complexes bind at the surface of $poly[d(G-C)_2]$, probably electrostatically to phosphate group. The results indicate that ${\Delta}{\Delta}$- and ${\Lambda}{\Lambda}-[{\mu}-Ru_2(phen)_4(bip)]^{4+}$ are able to discriminate between AT and GC base pairs.

• Molecules and Cells
• /
• v.26 no.2
• /
• pp.206-211
• /
• 2008

HI0381 of Haemophilus influenzae was investigated by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. HI0381 is a 153-residue peptidoglycan-associated outer membrane lipoprotein, and a part of the larger Tol/Pal network. Here, we report its backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments, and secondary structure predictions. About 97% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances covering 131 non-proline residues of the 134 residue, mature protein, were clarified by sequential and specific assignments. CSI and TALOS analyses revealed that HI0381 contains five ${\alpha}$-helices and five ${\beta}$-strands. To characterize the structure of HI0381, the effects of pH and salt concentration were investigated by CD. In addition, the structural changes occurring when HI0381 was in a membranous environment were investigated by comparing its HSQC spectra and CD data in buffer and in DPC micelles; the results showed that helix ${\alpha}4$ and strand ${\beta}4$ became aligned with the membrane. We conclude that the conformation of HI0381 is affected by the membrane environment, implying that its folded state is directly related to its function.

• BMB Reports
• /
• v.40 no.5
• /
• pp.783-790
• /
• 2007

Receptor binding plays an important role in determining host specificity of the Bacillus thuringiensis Cry $\delta$-endotoxins. Mutations in domains II and III have suggested the participation of certain residues in receptor recognition and insect specificity. In the present study, we expressed the cloned domain II-III fragment of Cry4Ba and examined its binding characteristics to mosquito-larval midgut proteins. The 43-kDa Cry4Ba-domain II-III protein over-expressed in Escherichia coli as inclusion bodies was only soluble when carbonate buffer, pH 10.0 was supplemented with 4M urea. After renaturation via stepwise dialysis and subsequent purification, the refolded domain II-III protein, which specifically reacts with anti Cry4Ba-domain III monoclonal antibody, predominantly exists as a $\beta$-sheet structure determined by circular dichroism spectroscopy. In vitro binding analysis to both histological midgut tissue sections and brush border membrane proteins prepared from susceptible Aedes aegypti mosquito-larvae revealed that the isolated Cry4Ba-domain II-III protein showed binding functionality comparable to the 65-kDa full-length active toxin. Altogether, the data present the 43-kDa Cry4Ba fragment comprising domains II and III that was produced in isolation was able to retain its receptor-binding characteristics to the target larval midgut proteins.