JPS595193A - Cyclic peptide - Google Patents
Cyclic peptideInfo
- Publication number
- JPS595193A JPS595193A JP11372682A JP11372682A JPS595193A JP S595193 A JPS595193 A JP S595193A JP 11372682 A JP11372682 A JP 11372682A JP 11372682 A JP11372682 A JP 11372682A JP S595193 A JPS595193 A JP S595193A
- Authority
- JP
- Japan
- Prior art keywords
- cyclic peptide
- formula
- powder
- ethanol
- present
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 102000001189 Cyclic Peptides Human genes 0.000 title claims abstract description 14
- 108010069514 Cyclic Peptides Proteins 0.000 title claims abstract description 14
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 claims 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 abstract description 10
- 231100000433 cytotoxic Toxicity 0.000 abstract description 5
- 230000001472 cytotoxic effect Effects 0.000 abstract description 5
- 238000004440 column chromatography Methods 0.000 abstract description 4
- 241000251557 Ascidiacea Species 0.000 abstract description 3
- 239000003795 chemical substances by application Substances 0.000 abstract description 3
- 239000000843 powder Substances 0.000 abstract description 3
- 239000000284 extract Substances 0.000 abstract description 2
- 230000003327 cancerostatic effect Effects 0.000 abstract 1
- 239000000463 material Substances 0.000 abstract 1
- 238000002360 preparation method Methods 0.000 abstract 1
- 238000010898 silica gel chromatography Methods 0.000 abstract 1
- 239000012265 solid product Substances 0.000 abstract 1
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 230000001093 anti-cancer Effects 0.000 description 4
- UHOVQNZJYSORNB-UHFFFAOYSA-N Benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 239000000741 silica gel Substances 0.000 description 3
- 229910002027 silica gel Inorganic materials 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- 230000000704 physical effect Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000005160 1H NMR spectroscopy Methods 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- 241000199914 Dinophyceae Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 101710138657 Neurotoxin Proteins 0.000 description 1
- 241001505332 Polyomavirus sp. Species 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 241000251555 Tunicata Species 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000000921 elemental analysis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000000469 ethanolic extract Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 125000001570 methylene group Chemical group [H]C([H])([*:1])[*:2] 0.000 description 1
- 239000002581 neurotoxin Substances 0.000 description 1
- 231100000618 neurotoxin Toxicity 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
Abstract
Description
【発明の詳細な説明】
本発明は、制癌性を有する新規な環状ブペチドに関する
。DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a novel cyclic bupetide having anticancer properties.
近年、海洋生物に関する研究が非常に活発に行われるよ
うにな？）、多くの成果が上げられている。In recent years, research on marine life has become very active. ), many results have been achieved.
海洋生物は、地上の生物とは異なる環境で生活しておｊ
ｌ−地十の生物とは異なる代謝機構を有しているものと
予想されているが、それを裏付けるように、海洋生物の
生体中から新規の骨格を有する化合物が多数発見されて
いる。Marine organisms live in environments different from those on land.
It is predicted that marine organisms have a metabolic mechanism different from that of other organisms, and in support of this, many compounds with novel skeletons have been discovered in marine organisms.
また、海洋生物の産生ずる毒成分の中には、例えば、赤
潮の原因である渦鞭毛藻類の産生ずるニューロトキンン
のように、生理的に興味のある活性を有するものも見出
されている。特に、海鞘綱（Ａｓｃｉｄｉａｃｅａ ）
に属する生物からは、強い細胞毒性又は制癌作用を有す
る環状ペプチドが見出されている。（Ｋ、Ｌ、 Ｒｌｎ
ｅｈａｒｔ ｅｔ ａｌ、 、 Ｊ 、Ａｍ、Ｃｈｅｍ
。Additionally, some toxic components produced by marine organisms have been found to have physiologically interesting activities, such as neurotoxin produced by dinoflagellates, which is the cause of red tide. . In particular, Ascidiacea
Cyclic peptides with strong cytotoxic or anticancer effects have been discovered from organisms belonging to the . (K, L, Rln
ehart et al., J. Am., Chem.
.
Ｓｏｃ、＋ １０３．１８７５（１９８１Ｌ Ｐ、Ｊ
、５ｃｂｅｕｅｒ ｅｉ、 ａｌ、、 ＪＡｍ、 Ｏｈ
ｅｍ、 Ｓｏｃ、、 １０２．５６８８（１９８０’）
）しかしながら、現在知られている環状ペプチドは数
種に過ぎず、動物種・部位・１ｍの種類等の相違による
多種の適用対象に、それぞれ対応しうるほどバラエティ
に富んではいない。Soc, + 103.1875 (1981L P, J
, 5cbeuer ei, al,, JAm, Oh
em, Soc, 102.5688 (1980')
) However, there are only a few types of cyclic peptides currently known, and they are not diverse enough to be applicable to a wide variety of applications due to differences in animal species, sites, types of 1m, etc.
本発明者らは、適用しつる範囲を拡げるため、更に、構
造の異なる制癌性環状ペプチドを見出すため、種々の海
洋生物について、広範な調査を行つた結果、オーストラ
リア・クィーンズランド・ローダ−リーフに生息する複
合ホヤ（ＣｏｍｐｏｕｎｄＡｓｃｉｄｉａｎ ）のエタ
ノール抽出物が、細胞毒性を有することを見出し、鋭意
器９℃の結果、本発明を完成したものである。In order to expand the scope of application and to find anticancer cyclic peptides with different structures, the present inventors conducted extensive research on various marine organisms, and found that It was discovered that the ethanol extract of Compound Ascidian, which lives in the United States, has cytotoxicity, and as a result of this experiment, the present invention was completed.
本発明は、下記式〔１〕で表わされる制）ｎｉ性を有す
る新規な環状ペプチドであり、本発明者らによＩＬ初め
て、単離精製されたものである。The present invention is a novel cyclic peptide having ni properties represented by the following formula [1], and is the first IL isolated and purified peptide by the present inventors.
本発明の環状ペプチドの物性は、次のとおＩ）である。The physical properties of the cyclic peptide of the present invention are as follows (I).
性状：無色プリズム様結晶
融点：１３９〜１３９．５℃
ＩＲ（フィルム、ｃｘ−’ ）： ３３８０．２９６０
゜１６８０．１６５２
ＵＶ（メタノ−）Ｌｔ ） ： ２３２ｎｍ （ｔ＝２
． ｔｏｏｏ）’ Ｈ−ＮＭＲ（ＯＤＣ］、３ 、ｌ
ｊ ｐｐｍ 、１００ＭＨｚ ）：８．０１（ＬＨ，ｄ
、Ｊ ＝８．１Ｈｚ）、７．９１（ＩＨ，８）７．４０
（ＬＨ，ｄ 、Ｊ＝１０Ｈｚ）、５．２２（ＩＨ。Properties: Colorless prism-like crystal Melting point: 139-139.5°C IR (film, cx-'): 3380.2960
゜1680.1652 UV (methano) Lt): 232nm (t=2
．． too)' H-NMR (ODC), 3, l
j ppm, 100MHz): 8.01 (LH, d
, J = 8.1Hz), 7.91 (IH, 8) 7.40
(LH, d, J=10Hz), 5.22 (IH.
ｄ ｄ 、Ｊ＝６．３．１０．０Ｈｚ）、４．８６（
ＩＨ，ｄｑ 。d d , J=6.3.10.0Hz), 4.86(
IH, dq.
Ｊ＝６．３ ．６．３Ｈｚ ）、４．８３（ＩＨ，ｄｄ
ｄ 、Ｊ＝８．１，６．１．１．２Ｈｚ）、４．２７（
ＩＨ，ｄｄ、Ｊ＝６．３．１．２Ｈｚ）、２．３１（Ｌ
Ｈ，ｄｑｑ 、Ｊ＝、６．３゜６．１．６．１Ｈｚ）、
１．９５（ＬＨ，ｍ）、１．４９（３Ｈ。J=6.3. 6.3Hz), 4.83(IH, dd
d, J=8.1, 6.1.1.2Hz), 4.27(
IH, dd, J=6.3.1.2Hz), 2.31(L
H, dqq, J=, 6.3°6.1.6.1Hz),
1.95 (LH, m), 1.49 (3H.
ｄ 、Ｊ＝６．３Ｈｚ ）、１．２７（ＬＨ，ｍ ）、
１．１７（ＩＨ，ｍ）、１．１３（３Ｈ，ｄ、、Ｔ＝６
．１Ｈｚ ）。d, J=6.3Hz), 1.27(LH,m),
1.17 (IH, m), 1.13 (3H, d,, T = 6
．． 1Hz).
１．０７（３［（、ｄ、Ｊ＝６．１Ｈｚ）、０．８０（
３）（。1.07(3[(,d,J=6.1Hz),0.80(
3)(.
ｔ 、Ｊ＝６．８Ｈｚ ）、０．７２ （３Ｈ、ｔ 、
Ｊ＝（ｉ、８Ｈｚ ）＋３０−ＮＭＲ（ＯＤＣ１３、δ
ｐｐｍ ） ： １７１２（Ｓ ）、１６８．９（Ｓ）
１１６８．４（Ｓ’）、１６０．３（Ｓ）、１４９．５
（Ｓ）、１２３．０（ｄ １，８１．５（（１）、７３
．５（ｄＬ５４．７（ｄ）、５２．０（ｄ）、３７．０
（ｄ）、３３．４（ｄ’）、２４．６（ｔｌ、２１．７
（ｑ）、１９．１（ｑ）。t, J=6.8Hz), 0.72 (3H, t,
J = (i, 8Hz) + 30-NMR (ODC13, δ
ppm): 1712 (S), 168.9 (S)
1168.4 (S'), 160.3 (S), 149.5
(S), 123.0 (d 1,81.5 ((1), 73
．． 5 (dL54.7 (d), 52.0 (d), 37.0
(d), 33.4 (d'), 24.6 (tl, 21.7
(q), 19.1(q).
１７．９（ｑ）、１４．９（ｑ）、ＩＯ，７（ｑ）ＭＳ
’Ｘ／ｚ（％） ７５６（Ｍ＋、７６ ）７１３
（Ｍ”−０Ｈ（ＯＨ３）２ 、１００ ）元素分析 ０
９ｆｌＨＡ２０６Ｎ８８２理論値 ０：５７．１２．ｆ
（：６．９２．Ｎ：１４．８０実測値 ０：５７．１３
．Ｈ：６．８６．Ｎ：１４．８５次に、本発明の環状ペ
プチドの単離精製法について、具体例によって説明する
。17.9(q), 14.9(q), IO, 7(q) MS
'X/z (%) 756 (M+, 76) 713
(M"-0H(OH3)2, 100) Elemental analysis 0
9flHA206N882 theoretical value 0:57.12. f
(:6.92.N:14.80 Actual value 0:57.13
．． H:6.86. N: 14.85 Next, the method for isolating and purifying a cyclic peptide of the present invention will be explained using a specific example.
採取した複合ホヤ（Ｃ！ｏｍｐｏｕｎｄ八５ｃｉｃ］ｉ
ａへ ）の凍結乾燥粉体４００ｇを、ガラスカラムに充
填し、エタノール２７１に浸し、３日間室温で静置し、
抽出した。抽出液を回収し、再び、同様な方法によ１］
、エタノール２１で抽出した。両袖出液を合わせて。Collected composite sea squirt (C! compound 85cic) i
Fill a glass column with 400 g of the freeze-dried powder of (a), immerse it in ethanol 271, and let it stand at room temperature for 3 days.
Extracted. Collect the extract and use the same method again 1]
, extracted with ethanol 21. Combine the fluid from both sleeves.
エタノールを／ｌ１ｉｌｉｌｆ留去し、固形物１６ｇ
を得た。Ethanol was distilled off to give 16g of solid matter.
I got it.
この固形物から、カラムクロマトグラフィ（担体、２３
０〜４００ メツシュシリカゲル。展開剤、塩化メチ
レン、メタノール（８０：１’）３によ１）、得られた
細胞毒性画分について、再び、ンリヵゲルカラムクロマ
トグラフィ（展開剤、塩化メチレン・メタノール（１０
０：ｌ）） を行い、細胞毒性両分を集めた。From this solid, column chromatography (carrier, 23
0-400 Metshu silica gel. The resulting cytotoxic fraction was again subjected to column chromatography on gel column chromatography (developing agent, methylene chloride/methanol (80:1')).
0:l)) and collected both cytotoxic fractions.
この両分から、中圧力ラムグロマトグラフイ（担体、シ
リカゲルＨ０展開剤、ベンゼン、アセトン（５：１））
によ（）、細胞毒性画分７００ｍ９ を得た。この両
分について、更に中圧力ラムグロマトグラフイ（担体、
シリカゲルＨ０展開剤、塩化メチレン・メタノール（１
００：１））を行い、該当画分から、本発明の環状ペプ
チド３８３ ＝９を得た。From these two parts, medium pressure ram chromatography (carrier, silica gel H0 developer, benzene, acetone (5:1))
(), a cytotoxic fraction of 700m9 was obtained. Both components were further analyzed by medium pressure lam chromatography (carrier,
Silica gel H0 developer, methylene chloride/methanol (1
00:1)), and the cyclic peptide 383 =9 of the present invention was obtained from the corresponding fraction.
次に、本発明の環状ペプチドの制癌性について、具体的
実験例によって説明する。Next, the anticancer properties of the cyclic peptide of the present invention will be explained using specific experimental examples.
実施例
バルブ／ｃ（ＢＡＬＢ／ｃ）由来のＡＳＩ細胞をポリオ
ーマウィルスによ１）変異させた癌化細胞（ＰＶ４）を
予め培養プレー＋１こ接種（−１種々の濃度の本発明の
環状ペプチドを含有する培養液によって、８日間培養し
た。その結果は１次の表のとお１］である。EXAMPLE BALB/c-derived ASI cells were inoculated with polyoma virus (1) mutated cancerous cells (PV4) into a culture plate +1 (-1 various concentrations of the cyclic peptide of the present invention). The cells were cultured for 8 days in a culture medium containing .The results are shown in the following table.
＊については、２８目に、すべての細胞が死滅している
のが確認された。Regarding *, it was confirmed that all the cells were dead at the 28th day.
手続軸正書（自発）
昭和５７年１０月２左目
特許庁長官 若 杉 和 人 殿１、事件の
表示
昭和５７年特許願第１１３７２６す
２、発明の名称
環状ペプチド
３、補正をする者
事件との関係 特許出願人
大阪市北区堂島浜２丁目１番４０吟
（１９０）サン１−リー株式会社
代表者 佐 治 敬 三
４、代理人
東京都港区元赤坂１−２−３
サントリー株式会社 技術特許室
明細書の「発明の詳細な説明」の欄
７・・″
７．７１正の内容
（１） 明８１１１書第３頁第８行「和製」を１製造
」と訂正する。Procedural axis book (spontaneous) October 2, 1981 Kazuto Wakasugi, Commissioner of the Left Eye Patent Office 1, Indication of the case 1981 Patent Application No. 113726-2, Name of the invention Cyclic peptide 3, Person making the amendment Case and Relationship Patent Applicant: 2-1-40 Gin (190) Dojimahama, Kita-ku, Osaka, Sun1-Re Co., Ltd. Representative: Keizo Saji 44, Agent: 1-2-3 Motoakasaka, Minato-ku, Tokyo Suntory Co., Ltd. Technology Column 7 of "Detailed Description of the Invention" in the Patent Office Specification 7.71 Correct Contents (1) Mei 8111, page 3, line 8, ``Made in Japan'' is corrected to ``1 manufacture''.
（２）同書第５頁第７行と第８行との間に、［なお、式
〔１〕に示される構造式は、上記物性の解析、及び、６
．ＩＮ塩酸で１０５ Ｃ２０時間加水分解すると、ス
レオニン、インロイシン等かえられることから、決定さ
れたものである。ｊを挿入する。(2) Between lines 7 and 8 of page 5 of the same book, the structural formula shown in formula [1] is based on the analysis of the above physical properties and 6
．． This was determined because threonine, inleucine, etc. are converted when 105C is hydrolyzed with IN hydrochloric acid for 20 hours. Insert j.
（３）同書同頁第８行及び第１０行の「単離精製」を１
製造」に訂正るる。(3) "Isolation and purification" in lines 8 and 10 of the same page of the same book as 1
Corrected to "Manufacturing".
Claims (1)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP11372682A JPS595193A (en) | 1982-06-30 | 1982-06-30 | Cyclic peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP11372682A JPS595193A (en) | 1982-06-30 | 1982-06-30 | Cyclic peptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS595193A true JPS595193A (en) | 1984-01-12 |
Family
ID=14619578
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP11372682A Pending JPS595193A (en) | 1982-06-30 | 1982-06-30 | Cyclic peptide |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS595193A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH09170680A (en) * | 1995-12-19 | 1997-06-30 | Hitachi Ltd | Piping support means and piping lug used in piping support means |
| WO2004074295A1 (en) * | 2003-02-21 | 2004-09-02 | Keio University | Thiazole cycle polymers, process for producing the same, synthesis intermediates thereof and utilization of the same |
-
1982
- 1982-06-30 JP JP11372682A patent/JPS595193A/en active Pending
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH09170680A (en) * | 1995-12-19 | 1997-06-30 | Hitachi Ltd | Piping support means and piping lug used in piping support means |
| WO2004074295A1 (en) * | 2003-02-21 | 2004-09-02 | Keio University | Thiazole cycle polymers, process for producing the same, synthesis intermediates thereof and utilization of the same |
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