• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.2
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• pp.244-251
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• 1997

The relationship between structure and biological activity was studied on the three neuropeptides (mammalian, trout- and goldfish-neuropeptide $\gamma$) that were syntheized by the solid-phase method. Circular dichroism spectra showed that mammalian, trout- and goldfish-neuropeptide $\gamma$ adopted an unordered structure in buffer solution. In the-presence of neutral and acidic liposomes, mammalian and trout-neuropeptioe $\gamma$ also took a random structure. However, goldfish-neuropeptide $\gamma$ took an $\alpha-helical$ structure in acidic liposomes. The intestinal motility response was investigated with carp intestines, guinea-pig ileums and rat duodenums. In case of carp intestine, contractile activity was as follows : goldfish-neuropeptide $\gamma\simeq$ trout-neuropeptide $\gamma>$ mammalian-neuropeptide $\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than trout- and goldfish-neuropeptide $\gamma$ in the guinea-pig ileums and rat duodenums. These results suggest that neuropeptide $\gamma$ show the species-specific activity.

• Journal of the Korean Chemical Society
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• v.25 no.5
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• pp.306-310
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• 1981

Induced circular dichroism spectra of racemic cobalt(III) complexes for $[Co(en)_3]^{3+},\;[Co(tn_)3]^{3+},\;cis-[Co(NH_3)(en)_2]^{3+},\;[Co({\beta}-ala)(en)2_]^{2+},\;[Co(gly)(en)_2]^{2+}\;and\;[Co(acac)(en)_2]^{2+}$ were measured when they were dissolved in aqueous d-tartrate2- solution at room temperature. Only a single negative CD spectrum was observed for all the complexes above in visible region(400∼500nm). It was interpreted that these CD bands were attributed to the difference in interaction between ${\Lambda}$-and ${\Delta}$-enantiomers with d-tartrate$^{2-}$. Namely, when d-tartrate$^{2-}$ was added to ${\Lambda}$-enantiomer and ${\Delta}$-enantiomer, it caused ${\Lambda}$-enantiomer to change greatly and ${\Delta}$-enantiomer to change only slightly; combined the results proved induced circular dichroism. The enantiomer for which the eluent has a stronger affinity should be eluted faster in ion-exchange column chromatography. It is possible to predict the elution order of chromatography from the sign of the induced CD if stronger interaction of chiral anion with the complex leads to greater change in the natural CD spectrum of the complex. The elution order was in complete agreement with the prediction from the sign of the induced CD spectrum for all the measured complexes.

• Journal of Life Science
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• v.27 no.5
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• pp.584-590
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• 2017

Antifreeze proteins (AFPs) bind to ice crystals and inhibit their growth. AFPs are essential for the survival of organisms living in subzero environments. Type I AFP (AFP37) isolated from winter flounder is an ${\alpha}$-helical peptide of 37 residues long. In this study, we attempted to develop short AFP fragments with higher activity and solubility. We designed and synthesized N-terminal 15 and 21 residue-long AFPs, designated AFP15 and 21. Also dimerized AFP15 and 21, designated dAFP15N and dAFP21N, respectively, were generated through disulfide bonds between peptides containing CGG residues added to the N-terminus of AFP15 and AFP21 (designated AFP15N and 21N). Their helical contents and antifreeze activities were assessed using circular dichroism (CD) spectroscopy and a nanoliter osmometer, respectively. The helical content of AFP15 AFP21, AFP15N, AFP21N, dAFP15N and dAFP21N was 47, 48, 23.8, 28, 49.1, and 52%, respectively compared to that of wild type AFP37; the antifreeze activity was 8.4, 9.3, 0.05, 5.6, 12.1, 11.2% respectively, compared to that of wild type AFP37. Contrary to our anticipation, the dimerized peptides showed almost the same antifreeze activity as their monomeric counterparts. These results indicate that the dimerized peptides behave as monomeric peptides due to the high rotational freedom of disulfide bonds connecting two monomeric peptides. The star-shaped ice crystals generated by the peptides also demonstrated weak interaction between ice and peptides.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.2
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• pp.232-237
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• 1999

The relationship between structure and contractile activity was studied on the three neuropeptide $\gamma$ (mammalian-, bowfin-, shark-NP$\gamma$) that were synthesized by the solid-phase method. Circular dichroism spectra showed that mammalian-, bowfin- and shark-neuropeptide $\gamma$ took an unordered structure in buffer solution and artificial liposome. The intestinal motility response was investigated with guinea-pig ileum, rat duodenum and carp intestine. In case of carp intestine, contractile activity was as follows; bowfin-NP$\gamma$> shark-NP$\gamma$>mammalian-NP$\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than those of bowfin-, shark-neuropeptide $\gamma$ in the guinea-pig ileum and rat duodenum. These results suggest that NP$\gamma$ show the species-specific activity.

• Journal of the Korean Chemical Society
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• v.39 no.2
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• pp.118-122
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• 1995

• Bulletin of the Korean Chemical Society
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• v.29 no.8
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• pp.1591-1593
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• 2008

• Journal of Pharmaceutical Investigation
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• v.14 no.3
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• pp.136-143
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• 1984

Inclusion complex formation of fenbufen with ${\beta}-cyclodextrin$ in water and in solid state was comfirmed by solubility method, ultra violet absorption, circular dichroism and infra-red spectroscopies, differential thermal analysis, and X-ray diffractometry. A solid complex of fenbufen with ${\beta}-cyclodextrin$ in 1 : 1 molar ratio was prepared by the freeze-drying method, its dissolution characteristics in water and its analgesic and antiinflammatory effect in mouse or rat were examined. The apparent release of fenbufen from the inclusion complex was significantly improved, hut no significant difference in its analgesic and antiinflammatory effect was found.

• Journal of Microbiology and Biotechnology
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• v.4 no.4
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• pp.364-366
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• 1994

Molecular properties of streptococcal nuclease purified from Streptococcus sp. were examined. The purified enzyme was stable in the range of pH 7 to 10 and easily inactivated above $60^{\circ}C$. Atomic spectroscopy analysis indicated that the enzyme contains Ca, Mg, Zn. Circular dichroism study showed 25% $\alpha$ -helix, 15% $\beta$-sheet and 30% $\beta$-tums.

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.25-25
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• 1996

A mature mutant ribose binding protein (RBP) of Escherichia coli was obtained by site-directed mutagenesis, replacing Thr-3 in the N-domain of wild-type mature RBP (WT -mRBP) with a Trp residue (N- Trp-mRBP). The equilibrium unfolding properties and the refolding kinetics of this protein were monitored by fluorescence and circular dichroism (CD). (omitted)

• Proceedings of the Korean Magnestics Society Conference
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• 2008.12a
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• pp.153.1-153.1
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• 2008