Vibrio Vulnificus Lipopolysaccharide의 생물활성과 그에 미치는 Cell Wall Protein-A의 영향

김용호,신홍대,강신원,Kim, Yong-Ho,Shin, Hong-Dae,Kang, Shin-Won 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.3

Vibrio(V.) vulnificus 대량 배양에 의하여 회수된 균체로부터 lipopolysaccharide(LPS)와 cell wall protein-A(CWP-A)를 추출하여 Sprague Dawley rat에서 생물활성을 생체의 독소 배설 기능에 관련된 장기의 효소 및 혈중 성분을 비교 측정한 결과 aspartate transaminase(AST), alanine aminotransferase(ALT) 및 blood urea nitrogen(BUN)은 LPS쪽의 활성이 높았으나 lactic dehydrogenase(LDH)는 CWP-A쪽이 훨씬 높았다. 기타의 측정군은 양자에서 모두 유사한 활성을 나타내었다. 따라서 숙주 혈중 순환 효소 및 성분의 변동 성향을 고려해 볼 때 V. vulnificus 병독성 해석에 내독소인 LPS 뿐만 아니라 CWP-A도 중요하게 고려되어야 한다고 본다. Lipopolysaccaride(LPS) and cell wall protein-A(CWP-A) were extracted from cell wall of Vibrio(V.) vulnificus. The biological activities of CWP-A were weaker than LPS in aspartate transaminase(ASP), alanine aminotransferase(ALT) and blood urea nitrogen(BUN), but more strong in lactic dehydrogenase(LDH) and very similiar in other test. CWP-A of V. vulnificus were considered to be important for the expression of virulence, LPS as well.

Vibrio Vulnificus Lipopolysaccharide 의 생물활성과 그에 미치는 Cell Wall Protein - A 의 영향

김용호,신홍대,강신원 ( Yong Ho Kim,Hong Dae Shin,Shin Won Kang ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.3

Lipopolysaccaride(LPS) and cell wall protein-A(CWP-A) were extracted from cell wall of Vibrio(V.) vulnificus. The biological activities of CWP-A were weaker than LPS in aspartate transaminase(ASP), alanine aminotransferase(ALT) and blood urea nitrogen(BUN), but more strong in lactic dehydrogenase (LDH) and very similiar in other test. CWP-A of V. vulnificus were considered to be important for the expression of virulence, LPS as well.

Cyclic Nona 및 Pentapetide 유도체들의 합성과 단백질 분해 효소에 대한 저해활성 측정

강신원,허남원,신홍대,Kang, Shin-Won,Huh, Nam-Won,Shin, Hong-Dae 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4

콩과식물의 씨속에 포함된 각종 BBI형 저해물질들은 reactive site를 중심으로 유사한 아미노산 잔기를 가지고 있다. 일반적으로 reactive site 내의 $P_1$ site 아미노산 잔기는 상대효소에 대한 특이성이 있다. Reactive site 뿐만 아니라 그 주변에 위치한 아미노산 잔기의 역할을 알아보기 위해 GBI-II의 antielastic fragment를 모델로 하여 $P_1$ site 아미노산 잔기를 치환시킨 3종의 cyclic nonapeptide를 액상법으로 합성하고 몇 종의 단백질 분해효소에 대한 $K_i$값을 Dixon 법으로 계산했다. GEI-II의 antielastic fragment $(I_a)$는 porcine pancreatIc 에라스타제에 대하여 $48{\mu}M$의 $K_i$값이 나타났고 LBI의 antitryptic fragment $(I_b)$는 트립신에 대한 $K_i$값이 $3.7{\mu}M$이었으며 Tyr 유도체인 $I_c$는 키모트립신에 대하여 저해활성이 없었지만 트립신과 에라스타제에 대하여 낮은 저해활성을 보였다. Loop size와 저해활성간의 관계를 알아보기 위해 $P_1$ site를 각각 Ala ($I_a$'), Lys ($I_b$') 및 Tyr ($I_c$')으로 치환시킨 3종의 cyclic pentapeptide를 합성하여 저해활성을 구한 결과 $I_a$'은 에라스타제에 대하여$614{\mu}M$, $I_b$'은 트립신에 대하여 $278{\mu}M$ 또한 $I_c$'은 키모트립신에 $128{\mu}M$의 $K_i$값으로 나타났다. Most of legume seeds contain serveral kinds of BBI-type inhibitors. They have similar amino acid residues around the reactive site. The $P_1$ site amino acid residue in reactive site generally corresponds to the specificity of the cognate enzyme. It has also been noted the importance of $P_1$ site amino acid residue in synthetic cyclic nonapeptide derivatives which were related to active site of BBI. To obtain further understanding of the role of amino acid residues near th reactive site, 3 cyclic nonapeptides which are substituted analogues of GBI-II were synthesized and the inhibition constants for some proteinases were calculated by Dixon method. Antielastic fragment in GBI-II $(I_a)$ differ only $P_2$' Site with that of soybean isoinhibitor C-II, Ki of Ia for porcine pancreatic elastase was $48{\mu}M$, Ki of antitryptic fragment in LBI $(I_b)$ for trypsin was $3.7{\mu}M$ and Tyr analogue $(I_c)$ for chymotrypsin showed no inhibition but appeared low inhibitory activity for trypsin and elastase. To elucidate the relation between loop size and inhibitory activity, 3 cyclic pentapeptide analogues containing the each reactive site of Ala-Ser, Lys-Ser and Tyr-Ser were synthesized. These peptides possessed slight inhibitory activity toward proteinases, Ki of synthetic cyclic pentapeptides for elastase, trypsin, and chymotrypsin were $614{\mu}M$, $278{\mu}M$ and $128{\mu}M$, respectively.

Cyclic Nona 및 Pentapeptide 유도체들의 합성과 단백질 분해 효소에 대한 저해활성 측정

강신원,허남원,신홍대 ( Shin Won Kang,Nam Won Huh,Hong Dae Shin ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4

Most of legume seeds contain serveral kinds of BBI-type inhibitors. They have similar amino acid residues around the reactive site. The P₁ site amino acid residue in reactive site generally corresponds to the specificity of the cognate enzyme. It has also been noted the importance of P₁ site amino acid residue in synthetic cyclic nonapeptide derivatives which were related to active site of BBI. To obtain further understanding of the role of amino acid residues near th reactive site, 3 cyclic nonapeptides which are substituted analogues of GBI-II were synthesized and the inhibition constants for some proteinases were calculated by Dixon method. Antielastic fragment in GBI-II (I_a) differ only P₂ Site with that of soybean isoinhibitor C-II, Ki of Ia for porcine pancreatic elastase was 48μM, Ki of antitryptic fragment in LBI (I_b) for trypsin was 3.7μM, and Tyr analogue (I_c) for chymotrypsin showed no inhibition but appeared low inhibitory activity for trypsin and elastase. To elucidate the relation between loop size and inhibitory activity, 3 cyclic pentapeptide analogues containing the each reactive site of Ala-Ser, Lys-Ser and Tyr-Ser were synthesized. These peptides possessed slight inhibitory activity toward proteinases, Ki of synthetic cyclic pentapeptides for elastase, trypsin, and chymotrypsin were 614μM, 278μM and 128μM, respectively.

누클레오시드 유도체의 약품 구상 , 합성 및 생리 활성 연구

문성환,김종안,김경희,구자석,허남원,김동규,신홍대,강신원 ( Sung Hwan Moon,Jong Ahn Kim,Keung Hee Kim,Ja Seok Koo,Nam Won Huh,Dong Kyu Kim,Hong Dae Shin,Shin Won Kang ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.4

Six new uridine-conjugates of penicillin G and peptides have been prepared and evaluated against mouse lymphoblastoma L5178Y cells, Staphylococcus aureus(IAM 3610) and Escherichia coli (ATCC 10536). These include 5`-amino-5`-deoxyuridine-penicillin G(14), 5`-amino-5`-deoxyuridine-cyclo(Phe-Asp)(15-I), 5`-amino-5`-deoxyuridine-cyclo (Phe-Glu)(15-II), 5-iodo-5`-amino-2`,3`-0-isopropylidene uridine-penicillin G(16), 5-iodo-5`-amino-5`-deoxyuridine-penicillin G(17), and 5`-deoxyuridine-penicillin G(19). IC_(50) values were 18.0 ㎍/㎖, 6.5 ㎍/㎖, 6.5 ㎍/㎖, 13.5 ㎍/㎖, 6.5 ㎍/㎖ and 9.0 ㎍/㎖, respectively. MIC values of (15-I) and (17) were 6.25 ㎍/㎖. These preliminary results support the thesis that the uridine conjugates of this type may require a naturally occuring moiety for improved efficacy.

Studies on the effective acyl residues of acylamino acids for the action of aminoacylases

Kang, Shin Won,Park, Jang Su,Jang, Tae Sik,Shin, Song Yub,Shin, Hong Dae 부산대학교 1984 자연과학논문집 Vol.38 No.-

The most effective acyl residue of substrates for mold aminoacylase was formyl group which has atronger electronegativiy than acetyl group and has the least molecular size compared with other acyl groups tested. In the case of aminoacylase Ⅰthe most appropriate acyl residue was butanoyl group which has almost the same electronegativity but larger molecular size than acetyl group.

아실아미노산에 관한 핵자기공명 연구 (Ⅰ)

姜信源,申洪大,金光鎬 부산대학교 1980 論文集 Vol.29 No.2

Various acyl derivatives of L-alanine, L-leucine and L-serine were synthesized. The relative electronegativity of various acyl residue was able to be evaluated from the data of chemical shift of amide proton of acylamino acids by ^(1)H-NMR measurement and a linear relationship existed between the chemical shift of amide proton of acylamino acids and PK_(a) value of the parent carboxylic acids of acyl residues.

1 , 2 - bis ( aminoacyl ) hydrazine 유도체들의 합성과 항산화 효과

강신원,이상운,신홍대 한국유화학회 1986 한국응용과학기술학회지 Vol.3 No.1

1.2-bis(aminoacyl) hydrazine derivatives and dipeptides were synthesized by conventional peptide synthesis procedures. Their antioxidant activity were inverstigated by over-storage test using corn oil as substrte. 1.2-bis (aminoacyl) hydrazine derivatives and dipetides containing hydrophobic side chain amino acid showed higher antioxidant activity. A free N-terminal amino group was also found to be important for the appearance of antioxidant activity. 1.2-bis (aminoacyl) hydrazine derivatives showed higher antioxidant activity than dipeptides. Antimicrobial activites of dipeptides and 1.2-bis (aminoacyl) hydrazine derivatives were also examined by the paper disc method. All of these compounds had shown no antimicrobial activity.