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Koock,Soon Uoong,Hong,Nam Joo,Park,Yeong Taek,Park,Doo Chun 國立 昌原大學校 産業技術硏究所 1990 産技硏論文集 Vol.4 No.-
The log P value of 16 N-acety1-di-and tripeptide amides composed of amino acids having unionizable side chanins was measured in a 1-octano1/pH 7.0 aqueous buffer system. The factors governing the variations in the log P value among these protected peptides were quantitatively analyzed physicochemical and substructural parameters. The log P value was governed by the sum of the hydrophobicity of side chains and the backbone as well as by the steric effects of side chains, the log P value was also affected by the "polar proximity factor" and/or intramolecular hydrogen bond formation in a way similar to that of zwitterionized peptides reported previously.
2-브로모프로피오닐화된 수지를 이용한 인슐린 A (1-21) 사슬의 합성
국순웅,홍남주,Soon Uoong Koock,Nam-Joo Hong 대한화학회 1987 대한화학회지 Vol.31 No.5
2-브로모프로피오닐화된 수지를 이용해 insulin A (1-21) 사슬을 합성하였다. 시스테인의 결사슬은 각각 acetamidomethyl, benzyl, 그리고 benzhydryl기로 보호하였으며 그루타민과 아스파라긴은 p-nitrophenyl기로 활성화하여 합성에 이용하였다. 매 짝지음단계마다 DCC/HOBT coupling agent로 각 아미노산을 축합하였으며 반응의 완결여부는 닌히드린시험으로 측정하였다. 생성물은 NH$_3$/MeOH-Dioxane(v/v 1:1)로 수지로부터 분리하여 DEAE Sephadex A-25와 Sephadex LH-20으로 정제하였으며 최종생산물은 HPLC, electrophoresis로 확인한 결과 순수한 것(>99.9%)으로 나타났으며 총수득율은 6%이었다. 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%.
회전반응 용기를 이용한 insulin B ( 5 - 9 ) analog 의 고체상 합성
국순웅,홍남주,신승동 ( Soon Uoong Koock,Nam Joo Hong,Seung Dong Shin ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.4
A simple, inexpensive apparatus has been designed to perform the solid-phase peptide synthesis. It consists of 60 ㎖ capacity glass cylinder (5×6 ㎝) fritted filter disc embeded in the flask and a one-way 1.5 ㎜ stopcock. The rotary reactor was used to avoid splashing any resin particles up on the sides of the vessel. This peptide synthesizer proved to be both reliable and convenient dining synthesis of the human insulin B (5-9) analog as a model compound. All coupling steps were monitored by ninhydrin procedure. The siolated peptide mixture resulting from Beyerman cleavage (Beyerman, 1979) was analyzed by HPLC and $gt;98% purity of the total product was shown to be the desired products.
Application of BMPI / HOBT Reagent in Solid-Phase Peptide Synthesis
홍남주,최수관,국순웅,Hong Nam Joo,Choi Soo Kwan,Koock Soon Uoong Korean Chemical Society 1989 Bulletin of the Korean Chemical Society Vol.10 No.1
The suitability of BMPI (2-bromo-N-methyl pyridinium iodide) for solid-phase peptide synthesis was investigated. The coupling rate of BMPI/HOBT procedure. BMPI/HOBT was superior to DCC/HOBT couplings using the solid-phase peptide bond formation proceeded to a greater degree of completion than DCC/HOBT method did. Double couplings with 2 equiv. of Bocamino acids and 1.5 equiv. of BMPI and $NEt_3$ and 2 equiv. of HOBT in DMF/MC (1:1 v/v) gave the best result for the preparation of a model compound. Stepwise solid phase peptide synthesis using BMPI/HOBT procedure was successfully utilized for the preparation of $(D-Ala)^2$-dynorphine A. BMPI/HOBT procedure for the synthesis of $(D-Ala)^2$-dynorphine gave better yield (20%) than DCC/HOBT procedure did.
Synthesis and Their Biological Activity of Carboxyl Terminal Extended Dermorphin Analogues
홍남주,정재규,국순웅,Hong, Nam-Joo,Cheong, Chae-Kyu,Koock, Soon-Uoong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
Dermorphin(H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser--$NH_2$)의 C-말단이 증가되면 그들의 opioidactivity가 어떻게 변화될 것인가를 알아보기 위해 Dermorphinoyl (DMR)-Arg, DMR-Arg-Arg,DMR-Arg-Arg-Val, DMR-Arg-Pro-Glu, ($Sar^4$)DMR-Arg, ($Sar^4$)DMR-Arg-Arg-Val, 그리고 ($Sar^4$) DMR-Arg-Pro-Glu를 합성하였다. Dermorphin 유도체들은 고상법으로 합성하였으며 그 정제된 유도체들을 생쥐의 정맥에 주사하여 hot-plate 시험법으로 진통효과을 측정하였다. 각 유도체에 대한 관측된 진통효과의 순서는 다음과 같다. Morphin>($Sar^4$)DMR-Arg-Arg-Val=DMR-Arg-Arg-Val>($Sar^4$)Dmr-Arg-Pro-Glu=DMR-Arg-Pro-Glu>($Sar^4$)DMR-Arg-Arg=DMR-Arg-Arg>($Sar^4$)DMR-Arg=DMR-Arg. Dermorphinoyl (DMR)-arginine, DMR-arginyl-arginine, DMR-arginylarginylvaline, DMR-arginyl-prolyl-glutamic acid, ($Sar^4$) DMR-arginine, ($Sar^4$) DMR-arginylarginine, ($Sar^4$) DMR-arginylarginyl-valine and ($Sar^4$) DMR-arginyl-prolyl-glutamic acid have been prepared in order to examine the effect of C-terminal extension of dermorphin (H-TyrD-Ala-Phe-Gly-Tyr-Pro-Ser-$NH_2$) on opioid activity. The dermorphin analogues were synthesized by the solid phase method. Following intravenous administration in mice (hot-plate test), the percent analgesic activities of compounds showed the following trend, morphin>($Sar^4$)DMR-Arg-Arg-Val=DMR-Arg-Arg-Val> ($Sar^4$)Dmr-Arg-Pro-Glu=DMR-Arg-Pro-Glu> ($Sar^4$)DMR-Arg-Arg=DMR-Arg-Arg> ($Sar^4$)DMR-Arg=DMR-Arg.
C - 말단이 증가된 Dermorphin 유도체의 합성과 생물학적 활성도
홍남주,정재규,국순웅 ( Nam Joo Hong,Chae Kyu Cheong,Soon Uoong Koock ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
Dermorphinoyl (DMR)-arginine, DMR-arginyl-arginine, DMR-arginylarginyl-valine, DMR-arginyl-prolyl-glutamic acid, (Sar⁴) DMR-arginine, (Sar⁴) DMR-arginyl-arginine, (Sar⁴) DMR-arginylarginyl-valine and (Sar⁴) DMR-arginyl-prolyl-glutamic acid have been prepared in order to examine the effect of C-terminal extension of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂) on opioid activity. The dermorphin analogues were synthesized by the solid phase method. Following intravenous administration in mice (hot-plate test), the percent analgesic activities of compounds showed the following trend, morphin$gt; (Sar⁴) DMR-Arg-Arg-Val = DMR-Arg-Arg-Val $gt; (Sar⁴) DMR-Arg-Pro-Glu = DMR-Arg-Pro-Glu $gt; (Sar⁴) DMR-Arg-Arg = DMR-Arg-Arg $gt; (Sar⁴) DMR-Arg = DMR-Arg.