• Bulletin of the Korean Chemical Society
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• v.23 no.11
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• pp.1527-1530
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• 2002

1,12-diazacyclodocosane-2,11-dione was first isolated from a plant Phyllanthus niruri Linn. Its structure has been determined by means of spectroscopy methods and X-ray crystallography. Two peptide groups in the big ring (lactam) are the main factors influencing intermolecular contacts. The hydrogen-bond interaction of these hydrophilic groups is observed in the crystal structure. Meanwhile, C-H···O hydrogen bonds in molecules contribute to the formation of the whole crystal. These two kinds of hydrogen-bond form six- member rings among molecules. This compound crystallizes in the triclinic space group P-1 with a= 9.588(1) $\AA$, b= $9.850(1)\AA$, c = $11.810(1)\AA$, $\alpha=$ 68.18(1)$^{\circ}C$ , $\beta=$ 84.98(1), $\gamma$ = 86.03(1)$^{\circ}C$ , V = $1030.66(17)\AA3$ , Z = 2. A disorder of five-member carbon chain in the whole ring is observed in the title compound. The bond angle 105.8(4) is determined for a extreme configuration C(14)-C(15)-C(16), and 117.7(10) for another extreme configuration C(14')-C(15')-C(16'). In this crystal, two molecules are tied each other by short intermolecular hydrogen bonds, the oxygen atom being tied by hydrogen bond to nitrogen atom of another two molecules. The NMR and IR spectral data coincides to the structure of the compound.

• Korean Journal of Microbiology
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• v.39 no.2
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• pp.83-88
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• 2003

We cloned a gene encoding acetyl xylan esterase(axeA) of Streptomyces coelicolor A3(2) and studied its expression pattern in Escherichia coli. The full sequence of axeA was amplified by PCR. Sequence analysis of the PCR product revealed an open reading frame of 1,008 nucleotides encoding a protein consisted of 335 amino acid residues, with a calculated molecular mass of about 38 kDa. The base sequence showed 98% homology to the same gene of Streptomyces lividans. Two different kinds of acetyl xylan esterases were produced in Escherichia coli(pLacI) by IPTG induction; their molecular weights were 38 kDa and 34 kDa, respectively. Of these, 38 kDa protein seemed to be a total protein holding N-terminal signal peptide region, whereas 34 kDa protein seemed to be a matured protein without signal peptide which was produced by peptide bond cleavage between two amino acid residues of alanine 41 and alanine 42.

• BMB Reports
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• v.35 no.3
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• pp.291-296
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• 2002

Thanatin, a 21-residue peptide, is an inducible insect peptide with a broad range of activity against bacteria and fungi. It has a C-terminal disulfide loop, like the frog skin secretion antimicrobial peptides of the brevinin family. In this study, we tried to find the effect of a number of amino acids between the disulfide bond. Thanatin showed stronger antibacterial activity to Gram negative bacteria than other mutants, except Th1; whereas, the mutant peptides with deletion had higher activity to Gram positive bacteria than thanatin. An increase in the number of amino acid(s) using the alanine residue decreased the antibacterial activity in all of the bacteria. Th1 with deletion of threonine at position 15 ($Thr^{15}$) showed similar antibacterial activity against Gram-negative bacteria, but had higher activity against the Gram positive bacteria. In order to study the structure-function relationship, we measured liposome disruption by the peptides and CD spectra of the peptides. Th1 also showed the highest liposome leaking activity and α-helical propensity in the sodium dodecyl sulfate solution, compared with other peptides. Liposome disruption activity was closely correlated with the anti-Gram positive bacterial activity. All of the peptides showed no hemolytic activity. Th1 was considered to be useful as an antimicrobial peptide with broad spectrum without toxicity.

• Korean Journal of Metals and Materials
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• v.46 no.1
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• pp.6-12
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• 2008

Peptides with specific sequences against $LaPO_4$ and $TiO_2$ nanoparticles were discovered through peptide phage display technique as an application to biomolecular recognition of inorganic materials. Sequencing results showed that a motif consisting of serine and proline was commonly expressed in specific sequences. It was postulated that serine directly bound to nanoparticles using its terminal hydroxyl (OH) group. In this sense, oxygen atom seemed to work as a ligand to metal ions and hydrogen atom as a H-bond donor, was thought to bind to the oxygen atoms or the hydroxyl groups on particle surface. Also, it was expected that proline assists serine to make an ideal van der Waals contact between serine and nanoparticles, which optimizes the binding of peptide onto surface.

• Journal of the Korean Chemical Society
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• v.31 no.5
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• pp.457-463
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• 1987

The total synthesis of insulin A chain (1-21) with properly protected sulfhdryl groups of three cysteins for the correct intra and inter disulfide bond formation has been accomplished on 2-bromopropionylated 2% DVB-styreneresin support employing manually operated rotary vessel. The sulfhydryl groups of cysteins were protected with acetamidomethyl, benzyl, and benzhydryl respectively. Glutamine and asparagine were attached to the peptide chain by active ester coupling, all other amino acids were coupled with DCC/HOBT. The synthesized peptide was purified by DEAE Sephadex A-25 and gel filtration Sephadex LH-20. The final product was found to be homogeneous by HPLC, electrophoresis, and amino acid analysis. The overall yield of the pure isolated peptide was 6%.

• Journal of Life Science
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• v.10 no.2
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• pp.210-217
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• 2000

A kinetic profile of the catalytic domain of stromelysin-1 (SCD) using the fluorescent peptide substrate has been determined by the stopped-flow technique. The pH profile has a pH optimum of about 5.5 with an extended shoulder above pH 7. Three pKa values, 5.0, 5.7, and 9.8 are found for the free enzyme state and two pH independent Kcat/Km values of 4.1$\times$104 M-1 s-1 and 1.4$\times$104 M-1 s-1 at low and high pH, respectively. The profile is quite different in shape with other MMP family which has been reported, having broad pH optimum with two pKa values. The substrate specificity of SCD towards fluorescent heptapeptide substrates has been also examined by thin layer chromatography. The cleavage sites of the substrates have been identified using reverse-phase HPLC method.SCD cleaves Dns-PLA↓L↓WAR and Dns-PLA↓L↓FAR at two positions. However, the Dns-PLA↓LRAR, Dns-PLE↓LFAR, adn Dns-PLSar↓LFAR are cleaved exclusively at one bond. The double cleavages of Dns-PLALWAR and Dns-PLALFAR by SCD are in marked contrast to the close structurally related matrilysin. A notable feature of SCD catalysis agrees with the structural data that the S1' pocket of SCD is deeper than that of matriysin. The differences observed between SCD and matrilysin may form the basis of understanding the structural relationships and substrate specificities of the MMP family in vivo.

• KSBB Journal
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• v.8 no.3
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• pp.209-216
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• 1993

For the production of biodegradable polymers from microorganisms a bacterial strain producing a biopolymer was isolated from soil. The bacteriological characteristics of this strain and physicochemical Properties of the biopolymer produced were investigated. The bacterial strain was identified as an alkalophilic Alcaligenes sp. The Purified biopolymer treated with cetylpridinium chloride and acetone was identified as an acidic biopolymer having carboxyl groups and showed strong UV absorbance (at 210nm). The biopolymer was composed of 100% glutamic acid and glutamic acid existed as $\gamma$-polyglutamic acid($\gamma$-PGA) in the form of the $\gamma$-peptide bond. The equivalent weight of this $\gamma$-PGA was estimated about 350, indicating that one acidic fraction per 2.7 residue of $\gamma$-polyglutamic acid existed. The molecular weight was $6.5{\times}10^5$ Daltons.

• Bulletin of the Korean Chemical Society
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• v.34 no.9
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• pp.2640-2644
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• 2013

The all-hydrocarbon i,i+4 stapling system using an oct-4-enyl crosslink is one of the most widely employed chemical tools to stabilize an ${\alpha}$-helical conformation of a short peptide. This crosslinking system has greatly extended our ability to modulate intracellular protein-macromolecule interactions. The helix-inducing property of the i,i+4 staple has shown to be highly dependent on the length and the stereochemistry of the oct-4-enyl crosslink. Here we show that changing the double bond position within the i,i+4 staple has a considerable impact not only on the formation of the crosslink but also on ${\alpha}$-helix induction. The data further increases the understanding of the structure-activity relationships of this valuable chemical tool.

• 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.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.23 no.2
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• pp.33-47
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• 1997

단백질 또는 peptide bond를 가수분해하는 protease는 현재 산업의 각 분야에서 널리 응용되고 있으며, 사용범위가 점차 확산되고 있는 추세이다. 따라서 본 실험에서는 미생물이 생산하는 단백질분해효소를 분리 정제하여 그의 성질을 규명 및 skin turn-over 효과를 조사하였다.