• Natural Product Sciences
• /
• v.29 no.2
• /
• pp.113-119
• /
• 2023

Descurainia sophia seeds methanol extract showed significant anti-influenza activity and we tried to isolate anti-influenza compounds from the D. sophia extract. D. sophia seeds were extracted with 80% methanol and fractionated with n-hexane, ethyl acetate, CHCl₃ and n-butanol. The anti-influenza activity of each fraction was assessed using sulforhodamine B (SRB) method in A549 cells, human-derived lung cancer cells. The ethyl acetate and CHCl₃ fractions showed the most potent anti-influenza activity. Seven compounds were isolated from CHCl₃ fraction and identified 1-decanol (1), 2-(3,4-dihydroxy-2-methylenebutoxy)-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol (2), daucosterol (3), isorhamnetin (4), quercetin (5), sinapic acid (6), and helveticoside (7) by spectroscopic data such as UV, IR, ¹H-NMR, ¹³C-NMR and mass spectroscopy. Anti-influenza activities of isolated compounds were evaluated using SRB method in A549 cells. Compounds 3, 4 and 7 had significant anti-influenza activity in a dose-dependent manner.

• Journal of Magnetics
• /
• v.15 no.2
• /
• pp.61-63
• /
• 2010

We used $^1H$ nuclear magnetic resonance (NMR) to study the phase transitions and molecular dynamics in a characteristic ferroelectric liquid crystal with a carbon number n = 7, S-2-methylbutyl 4-n-heptyloxybiphenyl-4'-carboxylate (C7). The results were compared with those of our recent work on S-2-methylbutyl 4-n-octanoyloxybiphenyl-4'-carboxylate (C8), with a carbon number n = 8. While the recrystallization and isotropic phase transitions exhibited a first-order nature in the $^1H$ NMR spin-lattice and spin-spin relaxation measurements, a second-order nature was shown at the Sm-A - Sm-$C^*$ liquid crystalline phase transition. A soft-mode anomaly arising from the tilt angle amplitude fluctuation of the director, of which only a hint had been noticed in the C8 system, was manifested in the C7 system at this transition.

• Bulletin of the Korean Chemical Society
• /
• v.31 no.7
• /
• pp.1869-1874
• /
• 2010

By reducing PVP with $H_2NOH$.HCl and NaOH 2:2:1 mass ratios in aqueous ethanol, poly-N-vinyl pyrrolidone oxime [PVPO] was prepared with 92% yield. Applying the sol-gel concept, orthosilicic acid [OSA] was made by hydrolyzing TEOS with ethanol in 1:0.5 molar ratios using 1 N KOH aqueous solution as a catalyst. The OSA + PVPO + $_L$-Valine ($\alpha$-amino acid) were mixed with pure ethanolic medium in 1:2:2 mass ratios and refluxed at $78^{\circ}C$ and 6 pH for 6.5 h. A white residue of poly-N-vinyl pyrrolidone oximo-L-valyl-siliconate [POVS] appeared after 5 h. The heating of reaction mixture was stopped and the contents were brought to NTP. The residue formation of POVS was intensified with lowering a temperature and completely solidified within 5 h, was filtered using a vacuum pump with Whatmann filter paper no. 42. The residue of POVS was washed several times with 20% aqueous cold ethanolic solution and dried in vacuum chamber at $25^{\circ}C$ for 24 h. The MP was noted above $350^{\circ}C$. Structural and internal morphology were analyzed with IR and $^1H$-NMR, and SEM respectively. A drug loading and transporting ability of the POVS in water and at pH = 5 and 8 was determined chromatographically.

• Journal of the Korean Wood Science and Technology
• /
• v.30 no.1
• /
• pp.56-62
• /
• 2002

The air-dried bark of Salix rorida was extracted with acetone-water(7:3, v/v) and its extractives were concentrated with a vacuum evaporator. The extractives were fractionated with a series of n-hexane, chloroform, ethylacetate(EtOAc) and water on a separatory funnel. Each fraction was freeze-dried to give some dark brown powder. The EtOAc and water soluble fractions were chromatographed on a Sephadex LH-20 column using a series of aqueous methanol and ethanol-hexane mixture as eluents. The isolated compounds were tested with a cellulose TLC developed with TBA and 6% acetic acid and then visualized on UV lamp or sprayed with vanillin-HCl-EtOH. The purified compounds were flavonoids and their glycosides as follows:(+)-catechin, naringenin, salipurposide, aromadendrin, isosalipurposide, aromadendrin-7-O-𝛽-D-glucopy- ranoside and taxifolin-7-O-𝛽-D-glucopyranoside. The structures of each compounds were confirmed by ¹H-NMR, ¹³C-NMR and mass spectra.

• Molecules and Cells
• /
• v.24 no.3
• /
• pp.437-440
• /
• 2007

$OGL-20P^T$-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain $OGL-20P^T$, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of $OGL-20P^T$-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ${\alpha}$-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.

• Journal of the Korean Magnetic Resonance Society
• /
• v.13 no.2
• /
• pp.117-125
• /
• 2009

HP0062 is an 86 residue hypothetical protein from Helicobacter pylori strain 26695. HP0062 was identified ESAT-6/WXG100 superfamily protein based on structure and sequence alignment and also contains leucine zipper domain sequence. Here, we report the sequence-specific backbone resonance assignment of HP0062. About 97.7% of all $^1H_N,\;^{15}N,\;^{13}C_{\alpha},\;^{13}C_{\beta}\;and\;^{13}C=O$ resonances were assigned unambiguously. We could predict the secondary structure of HP0062 by analyzing the deviation of the $^{13}C_{alpha}\;and\;^{13}C_{\beta}$ chemical shifts from their respective random coil values. Secondary structure prediction shows that HP0062 consist of two ${\alpha}$-helices. This study is a prerequisite for determining the solution structure of HP0062 and can be used for the study on interaction between HP0062 and DNA and other Helicobacter pylori proteins.

• Journal of the Korean Magnetic Resonance Society
• /
• v.19 no.1
• /
• pp.49-53
• /
• 2015

MRA1997 is a 76-residue conserved hypothetical protein of Mycobacterium tuberculosis H37Ra, one of the most pathogenic bacterial species and the causative agent of tuberculosis. In this study, the sequence-specific backbone resonance assignment of MRA1997 was performed using NMR spectroscopy. Approximately 88.3% of the total resonances could be unambiguously assigned. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one ${\alpha}$-helix and five ${\beta}$-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.

• Journal of the Korean Magnetic Resonance Society
• /
• v.17 no.2
• /
• pp.105-110
• /
• 2013

HP1492 is a NifU-like protein of Helicobacter pylori (H. pylori) and plays a role as a scaffold which transfer Fe-S cluster to Fe-S proteins like Ferredoxin. To understand how to bind to iron ion or iron-sulfur cluster, HP1492 was expressed and purified in Escherichia coli (E. coli). From the NMR measurement, we could carry out the sequence specific backbone resonance assignment of HP1492. Approximately 91% of all resonances could be assigned unambiguously. By analyzing results of CSI and TALOS from NMR data, we could predict the secondary structure of HP1492, which consists of three ${\alpha}$-helices and three ${\beta}$-sheets. This study is an essential step towards the structural characterization of HP1492.

• Journal of the Korean Magnetic Resonance Society
• /
• v.25 no.2
• /
• pp.17-23
• /
• 2021

High mobility group protein B1 (HMGB1) is a highly conserved, non-histone, chromatin associated nuclear protein encoded by HMGB1 gene. HMGB1 proteins may be general co-factors in Hox-mediated transcriptional activation that facilitate the access of Hox proteins to specific DNA targets. It is unclear that the exact binding interface of Hoxc9DBD and HMGB1. To identify the interface and binding affinity of Hoxc9DBD and HMGB1 A-box, the paramagnetic probe, MTSL was used in NMR titration experiment. It is attached to the N-terminal end of HMGB1 A-box by reaction with thiol groups. The backbone assignment of HMGB1 A-box was achieved with 3D NMR techinques. The ¹⁵N-labeled HMGB1 A-box was titrated with MTSL-labeled Hoxc9DBD respectively. Based on the chemical shift changes we can identify the interacting residues and further map out the binding sites on the protein structure. The NMR titration result showed that the binding interface of HMGB1 A-box is around loop-1 between helix-1 and helix-2. In addition, the additional contacts were found in N- and C-terminus. The N-terminal arm region of Hoxc9DBD is the major binding region and the loop between helix1 and helix2 is the minor binding region.

• Journal of the Korean Magnetic Resonance Society
• /
• v.15 no.2
• /
• pp.175-186
• /
• 2011

Amyloid fibrils have long been known to be the well known ${\alpha}$-helix to ${\beta}$-sheet transition characterizing the conversion of cellular to scrapie forms of the prion protein. A very short sequence of Yeast prion-like protein, GNNQQNY (SupN), is responsible for aggregation that induces diseases. KSI-fused tandem repeats of SupN vector are constructed and used to express SupN peptide in Escherichia coli (E.Coli). A method for a production, purification, and cleavage of tandem repeats of recombinant isotopically enriched SupN in E. coli is described. This method yields as much as 20 mg/L of isotope-enriched fusion proteins in minimal media. Synthetic SupN peptides and $^{13}C$ Gly labeled SupN peptides are studied by Congo Red staining, Birefringence and transmission electron microscopy to characterize amyloid fibril formation. To get a better understanding of aggregation-structure relationship of 7 residues of Yeast prion-like protein, the change of a conformational structure will be studied by $^{13}C$ solid-state nmr spectroscopy as powder of both amorphous and fibrillar forms.