• 한국환경과학회지
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• 제6권2호
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• pp.189-194
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• 1997

Hornet venom의 독성 peptide인 mastoparan과 mastoparan-B를 solid phase peptide syn- thesis method로 합성한 후 이들과 phospholipid와의 상호작용, 이들의 항균 활성 및 용혈 활성 을 조사하였다. 두가지 독성 peptide 모두 중성 liposome에서 저 농도에서도 dye release를 유도할 수 있었다. 중성 liposome에 대한 mastoparan-B의 결합 친화도는 산성 liposome에서 보다 작았다. Mastoparan과 mastoparan-B는 두가지 모두 그람 양성 세균에 대하여 강한 항균 활성을 가지고 있었으나 그람 음성 세균에 대해서는 각각 약하거나 유력한 활성을 보였다. Mastoparan과 mastoparan-B는 5$\mu$M의 낮은 농도에서도 적혈구를 분해시키는 독성을 보였다.

• 한국환경과학회지
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• 제7권1호
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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.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1998년도 학술발표회
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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)

• 생명과학회지
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• 제13권4호
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• pp.463-472
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• 2003

제5인자와 지질막 phosphatidylserine과의 상호작용은 prothrombinase 복합체의 활성을 조절하는데 중요하다. 본 연구에서 제5인자의 지질 결합부위에 위치한 Trp2063과 Trp2064를 동시에 돌연변이 시킨 재조합 제5인자를 과발현 시키고 정제하였다. 돌연변이된 제5인자는 1-10%의 phosphatidylserine을 포함하는 지질막에서 아주낮은 활성을 보였다. surface plasmon resonance에 의해서 지질막과의 결합을 측정한 결과 돌연변이된 제5인자가 본래의 제5인자보다 고정된 지질막에의 결합이 현저하게 떨어지는 것을 관찰하였다. 제5인자가 phosphatidylserine을 포함하는 지질막에 높은 친화력으로 결합하기 위해서는 Trp2063과 Trp2064가 필수적이고 이러한 상호작용은 생리적인 phosphatidylserine 농도를 포함하는 지질막 위에서 prothrombinase 복합체의 형성에 필요하다는 결론을 내렸다.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1996년도 정기총회 및 학술발표회
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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)

• 생명과학회지
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• 제26권8호
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• pp.875-880
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• 2016

진핵세포의 원형질막은 외부환경으로부터 세포를 격리하는 물리적인 장벽뿐만 아니라, 선택적 물질수송, 신호전달등 중요한 기능을 수행한다. 원형질막의 세포질쪽 지질층은 주로 Phosphatidylethanolamine (PE), Phosphatidylserine (PS), Phosphatidylinositides (PIs) 등의 인지질로 구성되어 있는데, 다양한 단백질들이 이들과 직접 결합하거나 이들의 성질을 이용해 원형질막으로 위치된다. 본 연구에서는 원형질막의 안쪽 지질층에 존재하는 특정 인지질과 결합하여, 원형질막에 위치되는 단백질을 과발현시켰을 때 나타나는 세포의 모양변화를 분석하였다. 이를 위해 PS와 PI등과의 선택적 결합으로 원형질막에 위치하는 단백질들과 소수성 또는 정전기적 상호작용으로 원형질막으로 위치되는 단백질들을 HEK293T세포에 과발현시켜 보았다. 그 결과, 대조군으로 사용한 EGFP 단백질과 PI4P에 선택적으로 결합하는 EGFP-P4M-SidM단백질의 발현은 세포의 모양변화를 유도하지 않았다. 반면, PI(4,5)P₂에 결합하는 EGFP-PLCδ1(PH), PI(3,4,5)P₃에 결합하는 EGFP-AKT1(PH), PI4P와 PI(4,5)P₂에 결합하는 OSH2(PH)x2-EGFP의 발현은 세포의 크기가 줄어드는 수축현상이 일어나면서, Lamilapodia나 Filopodia가 형성되는 것을 확인할 수 있었다. 반면에, PS결합을 통해 원형질막에 위치되는 Lact-C2-EGFP과 소수성결합에 의해 원형질막에 위치되는 ApPDE4 long-form인 L(N20)-EGFP이나, 정전기적인 결합을 통해 원형질막으로 위치되는 ApPDE4 short-form인 S(N-UCR1-2)-EGFP단백질의 경우는 세포의 크기가 줄어드는 수축현상은 일어나지만 Lamilapodia나 Filopodia와 같은 모양변화는 나타나지 않는 것을 확인할 수 있었다. 본 연구를 통해, 특정 인지질에 결합하여 원형질막에 위치되는 단백질들이 각각의 인지질 결합 특성에 따라 분류 가능한 세포의 모양변화가 일어남을 확인할 수 있었다.

• Journal of Nutrition and Health
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• 제30권8호
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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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• 제61권2호
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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.

• 한국어병학회지
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• 제9권1호
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• pp.65-77
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• 1996

Tachyplesin I은 투구게로부터 단리된 항균성 펩티드이다. 인지질막에 대한 tachyplesin I의 작용 메카니즘을 조사하기 위해서 tachyplesin I 및 5개의 유도체를 액상법으로 합성하였다. 합성한 5개의 유도체는 [$Phe^2$]-tachyplesin I, [$Phe^{8,13}$]-techyplesin I, S-S결합을 가지지 않는 [$Cys(Acm)^{3,7,12,16}$]-tachyplesin I 및 [$Cys(Acm)^{3,7,12,16}$]-tachyplesin I 의 단편인 7(Acm)과 10(Acm)이다. 원편광이색성 (CD) 스펙트럼에서 tachyplesin I은 완충액에서 역평행 $\beta$-구조를 취하며 산성 지질막하에서는 완충액보다 약간 불규칙적인 구조를 가진다. Carboxyfluorescein 누출 실험결과 tachyplesin은 중성 및 산성 지질막과 강하게 상호 작용 하였다. 또한 형광 실험하에서는 펩티드의 소수성 부분이 인지질막의 내부에 존재하였다. 7(Acm) 및 10(Acm) 유도체를 제외한 모든 펩티드들은 lipopolysaccharide결합에 있어 거의 유사한 활성을 나타냈었다. 따라서 지질이중막은 tachyplesin I을 안정한 $\beta$-구조로부터 덜 규칙적인 구조로 구조적 변화를 유도한다고 여겨진다.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1997년도 춘계학술대회
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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.