• Macromolecular Research
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• v.12 no.1
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• pp.46-52
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• 2004

In a continuation of our previous studies on blood compatibility profiles of anion-substituted poly(vinyl alcohol) (PVA) membranes, in which hydroxyl groups have been replaced with carboxymethyl (C-PVA) and sulfonyl groups (S-PVA), we have studied the activation of complement components and the changes in white cell and platelet count in vitro and compared them with those of unmodified PVA, Cuprophane, and low-density polyethylene. Complement activation of fluid phase components, C3a, Bb, iC3b, and SC5b-9, and of bound phases, C3c, C3d, and SC5b-9, were assessed by enzyme-linked immunosorbent assay (ELISA) and immunoblot, respectively. The changes in the number of white cells and platelets following complement activation were counted using a Coulter counter. C-PVA and S-PVA activated C3 to a lesser extent than did PVA, which we attribute to the diminished level of surface nucleophiles of the samples. In addition, C- and S-PVA exhibit increased inhibition of Bb production, resulting in a decrease in the extent of C5 activation. Consequently, because of the reduced activation of C3 and C5, C- and S-PVA samples cause marked decreases in the SC5b-9 levels in plasma. We also found that the negatively charged sulfonate and carboxylate groups of the samples cause a greater extent of adsorbtion of the positively charged anaphylatoxins, C3a and C5a, because of strong electrostatic attraction, which in turn provides an inhibition of chemotaxis and activation of leukocytes. The ability to inhibit complement production, together with the binding ability of anaphylatoxins of the C- and S-PVA samples, leads to a prominent decrease in lysis of leukocytes as well as activation of platelets.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2002.08a
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• pp.90-90
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• 2002

Syndecans, transmembrane heparan sulfate proteoglycans, are coreceptors with integrin in cell adhesion process. It forms a ternary signaling complex with protein kinase C and phosphatidylinositol 4,5 bisphosphate (PIP2) for integrin signaling. NMR data indicates that cytoplasmic domain of syndecan-4 (4L) undergoes a conformational transition in the presence of PIP2, forming oligomeric conformation. The structure based on NMR data demonstrated that syndecan-4L itself forms a compact intertwined symmetric dimer with an unusual clamp shape for residues Leu$^{186}$ -Ala$^{195}$ . The molecular surface of the syndecan-4L dimer is highly positively charged. In addition, no inter-subunit NOEs in membrane proximal amino acid resides (Cl region) has been observed, demonstrating that the Cl region is mostly unstructured in syndecan-4L dimmer. However, the complex structure in the presence of PIP2 induced a high order multimeric conformation in solution. In addition, phosphorylation of cytoplasmic domain induces conformational change of syndecan-4, resulting inhibition of PKC signaling. The NMR structural data strongly suggest that PIP2 promotes oligomerization of syndecan-4 cytoplasmic domain for PKC activation and further induces structural reorganization of syndecan for mediating signaling network in cell adhesion procedure.

• Analytical Science and Technology
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• v.9 no.3
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• pp.270-278
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• 1996

Response mechanism for the chloride-selective membrane doped with 5, 10, 15, 20-tetraphenyl(porphyrinato)manganase(III) chloride(Mn(TPP)Cl) in PVC/DOS matrix is proposed by examining the visible spectra of the corresponding optode membrane. The visible spectra of Mn(TPP)Cl-doped membrane placed in aqueous solution show that the chloride ligand is easily replaced with water molecule. When other halogen ions, such as $F^-$, $Br^-$ and $I^-$, are added to the sample solution, they replace the water ligand, exhibiting distinctive change in the Soret band of Mn(TPP). On the other hand, bulky anions, such as SCN and salicylate, do not form a bond with the central metal. These results suggests that the potentiometric response of Mn(TPP)-based membrane results either from the ligand exchange (water with halides) at the central metal or from the counter ion exchange (chlorides with bulky lipophilic anions) around the positively charged porphyrin molecule in membrane phase. It was also noted that both hydration enthalpies of anions and their binding constants to Mn(TPP) play critical role in determining the potentiometric selectivity pattern of the membrane.

• Membrane Journal
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• v.25 no.5
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• pp.422-430
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• 2015

The present study announces that the pH value of seed coating solution makes a significant effect on the microstructure of silicalite-1 zeolite layer formed on ${\alpha}$-alumina support. Seed with an average diameter of 75 nm was dispersed in ethanol to prepare three kinds of seed coating solutions with different pH values, and dip-coated on the support. The pH value was controlled to be 2.2, 7.0, and 9.3, respectively. In the secondary growth process, pH 7 seed solution resulted an uniform, 3 to $4{\mu}m$ thick, completely covered, and 100 nm grained silicalite-1 zeolite separation layer. The uniformity and completeness were explained by a uniform, closely packed, multi-layered, and completely covered seed coating in the pH 7 condition. In the condition, ${\alpha}$-alumina support and seed are oppositely charged: support is positively charged (8.4 mV) and seed, negatively (-1.7 mV). The opposite charging induced a strong electrostatic attraction between seed and support, which made the good seed coating state. On the other hand, pH 2.2 and pH 9.3 seed solutions resulted non-uniform, partially covered, and around $1{\mu}m$ grained zeolite separation layer, since seed and support are the same sign charged in the conditions. The same sign charging induced a strong electrostatic repulsion between seed and support which caused a low coverage of seed. It could be concluded that the pH value of seed coating solution is a key parameter to determine the microstructure of silicalite-1 zeolite separation layer.

• Membrane Journal
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• v.30 no.5
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• pp.307-318
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• 2020

Conventional perfluorinated sulfonic acid membrane, Nafion is widely used for vanadium redox flow battery (VRFB). It is desired to prevent vanadium ion permeation through a membrane to retain the capacity, and to keep the cell efficiency of a VRFB. Highly proton conductive and chemically stable Nafion membranes, however, suffer from high vanadium permeation, which induce the reduction in charge and discharge capacity by side reactions of vanadium ions. In this study, to resolve the issue, silica nanoparticles, which are functionalized with 3-aminopropyl group (fS) are introduced to enhance the long-term performance of a VRFB by lowering vanadium permeation. It is expected that amine groups on silica nanoparticles are converted to positive ammonium ion, which could deteriorate positively charged vanadium ions' crossover by Gibbs-Donnan effect. There is reduction in proton conductivity may due to acid-base complexation between fS and Nafion side chains, but ion selectivity of proton to vanadium ion is enhanced by introducing fS to Nafion membranes. With the composite membranes of Nafion and fS, VRFBs maintain their discharge capacity up to 80% at a high current density of 150 mA/㎠ during 200 cycles.

• Journal of Life Science
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• v.16 no.1
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• pp.37-43
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• 2006

Gap junction is an ion channel forming between adjacent cells. It also acts as a membrane channel like sodium or potassium channels in a single cell. The amino acid residues up to the $10^{th}$ position in the amino (N)-terminus of gap junction hemichannel affect gating polarity as well as current-voltage (I-V) relation. While wild-type Cx32 channel shows negative gating polarity and inwardly rectifying I-V relation, T8D channel in which threonine residue at $8^{th}$ position is replaced with negatively charged aspartate residue shows reverse gating polarity and linear I-V relation. It is still unclear whether these changes are resulted from the charge effect or the conformational change of the N-terminus. To clarify this issue, we made a mutant channel harboring cysteine residue at the $8^{th}$ position (T8C) and characterized its biophysical properties using substituted-cysteine accessibility method (SCAM). T8C channel shows negative gating polarity and inwardly rectifying I-V relation as wild-type channel does. This result indicates that the substitution of cysteine residue dose not perturb the original conformation of wild-type channel. To elucidate the charge effect two types of methaenthiosulfonate (MTS) reagents (negatively charged $MTSES^-$ and positively charged $MTSET^+$) were used. When $MTSES^-$ was applied, T8C channel behaved as T8D channel, showing positive gating polarity and linear I-V relation. This result indicates that the addition of a negative charge changes the biophysical properties of T8C channel. However, positively charged $MTSET^+$ maintained the main features of T8C channel as expected. It is likely that the addition of a charge by small MTS reagents does not distort the conformation of the N-terminus. Therefore, the opposite effects of $MTSES^-$ and $MTSETT^+$ on T8C channel suggest that the addition of a charge itself rather than the conformational change of the N-terminus changes gating polarity and I-V relation. Furthermore, the accessibility of MTS reagents to amino acid residues at the $8^{th}$ position supports the idea that the N-terminus of gap junction channel forms or lies in the aqueous pore.

• Journal of the Korean Society for Marine Environment & Energy
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• v.8 no.2
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• pp.60-66
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• 2005

When external pressure higher than osmosis pressure is reversely derived into solution, its solvent is moved into the solution having lower concentration, which is called 'reverse osmosis'. We investigated the desalination application of deep ocean water using reverse osmosis pressure of $40-70\;kgf/cm^2$ We observed how to operational factor j like flow rate, water temperature and pressure have effect on efficiency of reverse osmosis membrane and salts rejection. Fluxes of reverse osmosis membrane are directly proportional to water temperature and pressure. However, salts rejection rates are positively correlated with pressure and inversely proportional to water temperature. Separation efficiencies of osmosis membrane for major elements such as $Mg^{2+},\;Ca^{+2},\;Na^+\;and\;K^+$ are as follows in a strong electrolysis solution like seawater; $Ca^{2+},\;Mg^{2+}>K^+>Na^+$. Rejection rates of $Mg^{2+}\;and\;Ca^{2+}$ that have high electric charges are over 99% and show positively correlation with water temperature. Rejection rates of $Na^+$ having low electric charge is observed to be 98%-99%, which rates is much lower than those of $2^+$ charged ions like $Ca^{2+}\;and\;Mg^{2+}$. Ion rejection rates of boron, B, are much low because boron is present il free state or gas phase in seawater. Boron concentration in desalination water is over criteria of Korean drinking water, 0.3 mg/L. However, we could satisfied with the criteria of drinking water under the operation condition like temperature $5^{\circ}C$ and pressure $70kgf/cm^2$, using the relationship that rejection rates of boron is proportional to pressure and is inversely proportional to water temperature

• BMB Reports
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• v.53 no.5
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• pp.260-265
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• 2020

Scorpion venom comprises a cocktail of toxins that have proven to be useful molecular tools for studying the pharmacological properties of membrane ion channels. HelaTx1, a short peptide neurotoxin isolated recently from the venom of the scorpion Heterometrus laoticus, is a 25 amino acid peptide with two disulfide bonds that shares low sequence homology with other scorpion toxins. HelaTx1 effectively decreases the amplitude of the K⁺ currents of voltage-gated Kv1.1 and Kv1.6 channels expressed in Xenopus oocytes, and was identified as the first toxin member of the κ-KTx5 subfamily, based on a sequence comparison and phylogenetic analysis. In the present study, we report the NMR solution structure of HelaTx1, and the major interaction points for its binding to voltage-gated Kv1.1 channels. The NMR results indicate that HelaTx1 adopts a helix-loop-helix fold linked by two disulfide bonds without any β-sheets, resembling the molecular folding of other cysteine-stabilized helix-loop-helix (Cs α/α) scorpion toxins such as κ-hefutoxin, HeTx, and OmTx, as well as conotoxin pl14a. A series of alanine-scanning analogs revealed a broad surface on the toxin molecule largely comprising positively-charged residues that is crucial for interaction with voltage-gated Kv1.1 channels. Interestingly, the functional dyad, a key molecular determinant for activity against voltage-gated potassium channels in other toxins, is not present in HelaTx1.

• Genomics & Informatics
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• v.2 no.3
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• pp.121-125
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• 2004

The purpose of this study was to investigate the use of decision tree for the classification of antimicrobial peptides. The classification was based on the activities of known antimicrobial peptides against common microbes including Escherichia coli and Staphylococcus aureus. A feature selection was employed to select an effective subset of features from available attribute sets. Sequential applications of decision tree with 17 nodes with 9 leaves and 13 nodes with 7 leaves provided the classification rates of $76.74\%$ and $74.66\%$ against E. coli and S. aureus, respectively. Angle subtended by positively charged face and the positive charge commonly gave higher accuracies in both E. coli and S. aureusdatasets. In this study, we describe a successful application of decision tree that provides the understanding of the effects of physicochemical characteristics of peptides on bacterial membrane.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.68-68
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• 2003

HP(2-20) (AKKVFKRLEKLEKLFSKIQNDK) derived from the N-terminus of Helicobacter pylori Ribosomal Protein L1 shows potent antimicrobial activity against bacterial, fungi and cancer cells without cytotoxic effect. In order to investigate the relationships between antimicrobial activity and the structures, several analogues have been designed and synthesized. The structures of these peptides in SDS micelles have been investigated using NMR spectroscopy and they revealed that analogue 3 has the longest, well-defined alpha-helix from Val5 to Trp19. NOESY experiments performed on HP and its analogues in nondeuterated SDS micelles show that protons in the indole ring of Trp16 are in close contact with methylene protons of SDS micelles. In order to probe the position of HP and its analogues relative to the SDS micelles, spin-labeled stearate was added. Large effects are observed for the chemical shifts and the intensities of Phe5, Glu9, Phe12, and Trp16 within the helix region by 16-doxylstearate. This result implies that 16-doxylstearate is located in the center of the micelles and the hydrophobic phase of the amphiphilic ${\alpha}$-helix is located in contact with the acyl chains of the micelles. Also, Lys3 and Lys4 at N-terminus and Lys20 at C-terminus may produce an optimal arrangement for electrostatic interactions between the sulfate head groups of the SDS and the positively charged lysyl N$\sub$3/$\^$+/. Interactions between the indole ring of Trp and the membrane, as well as the amphiphilic ${\alpha}$-helical structure of HP induced by Trp at the C-terminus may allow HP to span the lipid bilayer. These structural features are crucial for their potent antibiotic activities.