• Journal of Environmental Science International
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• v.6 no.2
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• pp.189-194
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• 1997

Toxic peptides from hornet venom, mastoparan and mastoparan-B were synthesized us- ing the solid phase peptide synthesis method and investigated the interaction of them with phospholipid bilayer, antibacterial activity, and hemolytic activity. Both toxic peptides could induce dye release at a low concentration in neutral liposome. The binding affinity of mastoparan-B for neutral liposome was smaller than that for acidic one. Mastoparan and mastoparan-B had strong antibacterial activity for gram-positive bacteria, but weak or potent activity for gram-negative ones, respectively. Mastoparan and mastoparan-B lysed erythrocyte very little up to 5 $\mu$M.

• Journal of Environmental Science International
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• v.7 no.1
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• pp.62-66
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• 1998

Toxic Mastoparan B(MP-B) which is purified from the venom of the hornet Vespa basalis is a cationic amphlphilic tetradecapeptide. MP-B and Its Ala-substituted analogues were synthesized by solld phase method and the toxic peptide-membrane interactions were examined by circular dichroism(CD) spectra, fluorescence spectra, and leakage abilities in phospholipid membranes. In the presence of phospholipid vesicles, synthetic MP-B and its analogues formed amphiphilic -helical structures, but in the buffer soletion, those exhibited random coil conformation as measured by CD. Fluorescence spectra of MP-B and its analogues which indicated the binding affinity of peptide on phospholipid vesicles showed that the replacement of Lys at position 2 and 11 with Ala caused a remarkable effect in the blue shalt and that at position 2, in the leakage ability of the peptide.

• Proceedings of the Korean Biophysical Society Conference
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• 1998.06a
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• pp.16-16
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• 1998

The role of phospholipids in the membrane binding and subsequent insertion of the microsomal protein rabbit cytochrome P450 (P450) lA2 into phospholipid bilayers was investigated. The insertion of P450 lA2 into phospholipid bilayers was determined by the amount of quenching of Trp fluorescence of P450 lA2 by pyrene and brominated and doxyl-labeled phospholipids.(omitted)

• Journal of Life Science
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• v.13 no.4
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• pp.463-472
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• 2003

Interactions between factor Va (HFVa) and membrane phosphatidylserine (PS) regulate the activity of the prothrombinase complex. I have previously shown that two solvent exposed hydrophobic residues located in the C2-domain, Trp2063 and Trp2064, are required for binding to immobilized PS and for expression of procoagulant activity on membranes containing 5% PS. In order to fully define the functional importance of these two residues I have expressed and isolated recombinant factor Va (rHFVa) W2063A/W2064A double mutant. In contrast to the native protein the two glycoforms resulting from alternative glycosylation of Asn2181 eluted as a single peak with rHFVa1 W2063A/W2064A eluting on the leading edge and rHFVa2 W2063A/W2064A eluting on the trailing edge. The double mutant rHFVa2 W2063A/W2064A expressed little or no procoagulant activity on membranes containing 1-10% mol % PS. In contrast, the procoagulant activity of this mutant was slightly greater than the native protein on membranes containing>18 mol % PS. The binding of rHFVa2 W2063A/W2064A to immobilized phospholipid vesicles was markedly reduced compared to the native protein in a surface plasmon resonance binding assay. I conclude that Trp2063 and Trp2064 are required for high affinity binding of factor Va to PS membranes and that this interaction is necessary for assembly of the prothrombinase complex on membranes containing physiological concentrations of PS.

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.17-17
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• 1996

Annexin I is a member of the annexin family of calcium dependent phospholipid binding proteins and has anti-inflammatory activity by inhibiting phospholipase A$_2$ (PLA$_2$). Recent X-ray crystallographic study of annexin I identified six Ca$\^$2+/ binding sites, which was different types (type II, III) from the well-known EF-hand motif (type I). (omitted)

• Journal of Life Science
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• v.26 no.8
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• pp.875-880
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• 2016

The plasma membrane plays a crucial role in relaying signals from the outside environment to the inside of the cells. In eukaryotic cells, the inner leaflets of the plasma membrane are composed mostly of phospholipids, including phosphatidylethanolamine (PE), phosphatidylserine (PS), and phosphatidylinositides (PIs). In this study, we tried to analyze the morphological changes induced by EGFP-fused membrane binding proteins, which are targeted to the plasma membrane via specific phospholipids binding. As a result, we found that overexpression of EGFP-P4M-SidM, a specific PI4P binding protein, or EGFP alone, did not induce any morphological changes. On the other hand, overexpression of EGFP-PLCδ1(PH), which is a specific PI(4,5)P₂ binding protein, EGFP-AKT1(PH) which binds to PI(3,4,5)P₃, or EGFP-OSH2(PH)×2 which binds to PI4P and PI(4,5)P₂, could induce the filopodia and lamilapodia formation as well as cell shrinkage. Overexpression of Lact-C2-EGFP which is a specific PS-binding probe, EGFP fused Aplysia phosphodiesterase 4 (ApPDE4) long-form (L(N20)-EGFP) which is localized to the plasma membrane via hydrophobic interaction, or EGFP fused Aplysia PDE4 short-form (S(N-UCR1-2)-EGFP) which is localized to the plasma membrane via electrostatic interaction, could induce cell shrinkage, but not filopodia or lamilapodia formation. Taken together, our data support that the different phospholipid bindings in the plasma membrane could induce different characteristic morphological changes. Thus, we can analyze, characterize, and classify the cellular morphological changes induced by the various phospholipid binding proteins.

• Journal of Nutrition and Health
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• v.30 no.8
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• pp.930-935
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• 1997

Fatty acid binging proteins(FABP) are distinct but related gene productes which are found in many mamalian cell types. FABP bind long chain fatty acids in vitro. However, their functions and mechanisms of action, in vivo, remain unknown . Also not known is whether all FABP function similaryly in their respective cell types. or whether different FABP have unique functions. The puropose of the present study was to assess whether different members of the FABP family exhibit different structural and function properties. A comparison was made between heart(H-FABP) and liver (L-FABP). The results show that the binding sites of both FABP are hydrophobic in nature, although the L-FABP site is more nonpolar than the H-FABP site. Additionally, the bound ligand experiences less motional constraint within the H-FABP binding site than within the L-FABP binding site. In accordance with these differences in structural properties, it was found that anthroyloxy-fatty acid transfer from H-FABP to membranes is markedly faster than from L-FABP. moreover, the mechanism of fatty acid transfer to phospholipid membranes appears to occur via transient collisional interactions between H-FABP and membranes. In contrast , transfer of fatty acid from L-FABP occurs via an aqueous diffusion mechanism.

• Journal of Animal Science and Technology
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• v.61 no.2
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• pp.69-76
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• 2019

Maize which has very high omega-6 fatty acid content has been used as a main feed grain for Hanwoo beef production to increase marbling, and thus omega-6 to omega-3 fatty acids ratio in Hanwoo beef is expected to be biased. To elucidate the current status of omega fatty acids ratio in Hanwoo beef, fatty acid profiles of neutral lipid and phospholipid fraction were analyzed separately using 55 Hanwoo steers' longissimus dorsi muscle slaughtered at Pyeongchang, Korea from Oct. to Nov. 2015. In addition, an association study was conducted to evaluate associations between single nucleotide polymorphism (SNP) markers from references and omega fatty acid profiles in phospholipid of Hanwoo beef samples using analysis of variance (ANOVA). In neutral lipid fraction, composition of saturated and monounsaturated fatty acids was higher and polyunsaturated fatty acids was lower compared to those in phospholipid fraction. The mean n-6/n-3 ratios of Hanwoo were $56.059{\pm}16.180$ and $26.811{\pm}6.668$ in phospholipid and neutral lipid, respectively. There were three SNPs showing statistically significant associations with omega fatty acid content. GA type of rs41919985 in fatty acid synthase (FASN) was significantly associated with the highest amount of C20:5 n-3 (p = 0.031). CC type of rs41729173 in fatty acid-binding protein 4 (FABP4) was significantly associated with the lowest amount of C22:2n-6 (p = 0.047). AG type of rs42187261 in FADS1 was significantly linked to the lowest concentration of C20:4 n-6 (p = 0.044). The total n-6/n-3 ratio of the steer which has all four SNP types in above loci (27.905) was much lower than the mean value of the total n-6/n-3 ratio in phospholipid of the 55 Hanwoo steers ($56.059{\pm}16.180$). It was found that phospholipid and neutral lipid of Hanwoo have very high n-6/n-3 ratios compared to the reported data from different cow breeds. Four SNPs in genes related with fatty acid metabolism showed significant associations with the fatty acid profile of phospholipid and may have potential as SNP markers to select Hanwoo steers in terms of n-6/n-3 balance in the future.

• Journal of fish pathology
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• v.9 no.1
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• pp.65-77
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• 1996

Tachyplesin I is an antimicrobial peptide isolated from horseshoe crab. To investigate the mechanism of action of tachyplesin I for phospholipid bilayers, tachyplesin I and five analogs have been synthesized by the solution method. The synthesized five analogs are [$Phe^2$]-tachyplesin I, [$Phe^{8,13}$]-tachyplesin I, [$Cys(Acm)^{3,7,12,16}$]-tachyplesin I with no disulfide bonds, 7(Acm) and 10 (Acm) which denote the fragments [$Cys(Acm)^{3,7,12,16}$]-tachyplesin I. Circular dichroism spectra showed that tachyplesin I took an antiparallel $\beta$-structure in buffer solution and a less ordered structure in acidic liposomes. The carboxyfluorescein leakage experiment indicated that tachyplesin I interacted strongly with neutral and acidic phospholipid bilayers. In fluorescence experiment, the hydrophobic part of the peptide was shown to be embedded in lipid bilayers. All the peptides except for 7(Acm) and 10(Acm) were almost equally active in lipopolysaccharide binding. Therefore, the present study suggested that phospholipid bilayers induced a conformational change of tachyplesin I from the stable $\beta$-structure to a less ordered one.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1997.04a
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• pp.86-86
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• 1997

Human annexin I is a member of annexin family of calcium dependent phospholipid binding proteins, which have been implicated in various physiological roles including phospholipase A$_2$ (PLA$_2$) inhibition, membrane fusion and calcium channel activity. In this work, the structure of N-terminally truncated human annexin I (Δ-annexin I) and its interactions with Ca$\^$2+/, ATP and cAMP were studied at atomic level by using $^1$H, $\^$15/N, $\^$l3/C NMR (nuclear magnetic resonance) spectroscopy. The effect of Ca$\^$2+/ binding on the structure of Δ-annexin I was investigated, and compared with that of Mg$\^$2+/ binding. The addition of Ca$\^$2+/ to Δ-annexin I caused some changes in the high field and low field regions of $^1$H NMR spectra. Whereas, upon addition of Mg$\^$2+/ to Δ-annexin I, almost no change could be observed. Also we found that the binding ratio of ATP to Δ-annexin I is 1. Because Δ-annexin I is a large protein with 35 kDa molecular weight, site-specific (carbonyl-$\^$l3/C, amide-$\^$15/N) labeling technique was used to determine the interaction sites of Δ-annexin I with Ca$\^$2+/ and ATP. Assignments of all the histidinyl carbonyl carbon resonances have been completed by using Δ-annexin I along with its specific 1,2-subdomain. The carbonyl carbon resonances originating from His52 and His246 of Δ-annexin I were significantly affected by Ca$\^$2+/ binding, and some Tyr and Phe resonances were also affected. The carbonyl carbon resonances originating from His52 is significantly affected by ATP binding, therefore His52 seems to be involved in the ATP binding site of Δ-annexin I.