JPH04208300A - New peptide - Google Patents
New peptideInfo
- Publication number
- JPH04208300A JPH04208300A JP2338643A JP33864390A JPH04208300A JP H04208300 A JPH04208300 A JP H04208300A JP 2338643 A JP2338643 A JP 2338643A JP 33864390 A JP33864390 A JP 33864390A JP H04208300 A JPH04208300 A JP H04208300A
- Authority
- JP
- Japan
- Prior art keywords
- peptide
- insect
- pro
- pheromone
- biosynthesis
- 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
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 20
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 claims abstract description 6
- 125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 claims abstract description 6
- 150000001413 amino acids Chemical class 0.000 claims description 2
- 241000238631 Hexapoda Species 0.000 abstract description 31
- 239000003016 pheromone Substances 0.000 abstract description 27
- 230000015572 biosynthetic process Effects 0.000 abstract description 19
- 239000000877 Sex Attractant Substances 0.000 abstract description 5
- 230000000694 effects Effects 0.000 abstract description 5
- 238000000034 method Methods 0.000 abstract description 5
- 238000004007 reversed phase HPLC Methods 0.000 abstract description 2
- 239000000463 material Substances 0.000 abstract 1
- 239000007790 solid phase Substances 0.000 abstract 1
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 abstract 1
- 230000001939 inductive effect Effects 0.000 description 17
- 108091005601 modified peptides Proteins 0.000 description 12
- 238000012360 testing method Methods 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 7
- CIVIWCVVOFNUST-VFABXPAXSA-N Bombycol Natural products C(CCCCCCCC\C=C\C=CCCC)O CIVIWCVVOFNUST-VFABXPAXSA-N 0.000 description 6
- 101800003163 Pheromone biosynthesis-activating neuropeptide I Proteins 0.000 description 5
- 241000255789 Bombyx mori Species 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 238000004166 bioassay Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 241000208125 Nicotiana Species 0.000 description 2
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 2
- 101500013104 Pelophylax ridibundus Secretoneurin Proteins 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 241000607479 Yersinia pestis Species 0.000 description 2
- 239000013543 active substance Substances 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- CIVIWCVVOFNUST-SCFJQAPRSA-N bombykol Chemical compound CCC\C=C/C=C/CCCCCCCCCO CIVIWCVVOFNUST-SCFJQAPRSA-N 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 210000004907 gland Anatomy 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 1
- 241000239290 Araneae Species 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- PASDCCFISLVPSO-UHFFFAOYSA-N benzoyl chloride Chemical compound ClC(=O)C1=CC=CC=C1 PASDCCFISLVPSO-UHFFFAOYSA-N 0.000 description 1
- 238000006480 benzoylation reaction Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 231100000086 high toxicity Toxicity 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 239000002917 insecticide Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000002574 poison Substances 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 235000020138 yakult Nutrition 0.000 description 1
Landscapes
- Agricultural Chemicals And Associated Chemicals (AREA)
- Peptides Or Proteins (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は、昆虫フェロモン生合成誘導活性を有する新規
ペプチドに関する。DETAILED DESCRIPTION OF THE INVENTION [Field of Industrial Application] The present invention relates to a novel peptide having insect pheromone biosynthesis-inducing activity.
従来、農作物等に被害を与える害虫を駆除するために、
殺虫物質等の昆虫制御物質が使用されている。しかしな
がら、近年の環境問題の深刻化に伴い、昆虫制御物質の
毒性の高さや自然環境中での分解性の低さから、昆虫制
御物質の残留毒による環境汚染が問題になっている。Conventionally, in order to exterminate pests that damage agricultural crops,
Insect control substances such as insecticides are used. However, as environmental problems have become more serious in recent years, environmental pollution due to the residual poisons of insect control substances has become a problem due to their high toxicity and low decomposability in the natural environment.
このような問題を解決するために、生物が本来有する生
体調節機構を巧みに利用した昆虫制御技術が検討されて
いる。このような昆虫制御技術の一つに、昆虫性フエロ
モンによって昆虫を誘引捕殺する方法等が検討されてい
る。In order to solve these problems, insect control techniques that skillfully utilize the biological regulation mechanisms inherent in living things are being studied. As one such insect control technology, a method of attracting and killing insects using insect pheromones is being considered.
しかしながら、昆虫性フエロモンは、化学的に不安定な
物質が多く、構造決定が難しい。また、昆虫性フエロモ
ンの多くは、光学活性物質であるので、化学的合成によ
る昆虫性フエロモンの製造は困難である。このため、多
くの昆虫を捕獲または飼育し、昆虫性フエロモンを抽出
する必要がある。しかし、昆虫は、常に大量の性フエロ
モンを生合成するわけではなく、季節、光条件、気温等
の要因によって性フエロモンの生合成量が変動する。こ
のため、常時、必要量の昆虫性フエロモンを製造するこ
とは困難であった。However, many insect pheromones are chemically unstable, making it difficult to determine their structures. Furthermore, since most insect pheromones are optically active substances, it is difficult to produce insect pheromones by chemical synthesis. Therefore, it is necessary to capture or raise many insects and extract insect pheromones. However, insects do not always biosynthesize large amounts of sex pheromones, and the amount of sex pheromones biosynthesized varies depending on factors such as season, light conditions, and temperature. For this reason, it has been difficult to constantly produce the required amount of insect pheromone.
このような観点から、本発明者は、昆虫性フエロモンの
生合成を誘導する物質を昆虫に投与して、必要な時期に
昆虫に性フエロモンを生合成させることを鋭意検討した
結果、先に蚕の脳から昆虫フェロモンの生合成誘導活性
を有する２種類の脳ペプチドを精製し、ＰＢＡＮ−Ｉ、
ＰＢＡＮ−ｎと名付けた。このうちＰＢＡＮ−１の化学
構造を、３３残基のアミノ酸からなる修飾ペプチドであ
ると決定した。更に、化学的に合成したこの修飾ペプチ
ドが、天然のＰＡＢＮ−Ｉと同一の昆虫フェロモン生合
成誘導活性を有することを明らかにした（バイオケミカ
ル・アンド・バイオフィジカル・リサーチ・コミュニケ
ーションズ Ｂｉｏｃｈｅｍ、Ｂｉｏｐｈｙｓ、Ｒｅｓ
、Ｃｏｍｍ、１６３． ５２０〜５２６ （１９８９）
）。From this point of view, the present inventors have conducted intensive studies on the idea of administering to insects a substance that induces the biosynthesis of insect pheromone to cause insects to biosynthesize sex pheromone at the required time. Two types of brain peptides with insect pheromone biosynthesis-inducing activity were purified from the brain of
It was named PBAN-n. Among these, the chemical structure of PBAN-1 was determined to be a modified peptide consisting of 33 amino acid residues. Furthermore, it was revealed that this chemically synthesized modified peptide has the same insect pheromone biosynthesis inducing activity as natural PABN-I (Biochemical and Biophysical Research Communications Biochem, Biophys, Res
, Comm, 163. 520-526 (1989)
).
ＰＢＡＮ−Ｉのアミノ酸配列は、下記の通りである。The amino acid sequence of PBAN-I is as follows.
Ｈ−Ｌｅｕ−８ｅ ｒ−Ｇ Ｉ ｕ−Ａｓ ｐ−Ｍｅｉ
−Ｐ ｒｏ−Ａ ｌ ａ−Ｔｈ ｒ−Ｐ ｒｏ−Ａ Ｉ
ａ−Ａｓ ｐ−Ｇ Ｉ ｎ−Ｇ Ｉ ｕ−Ｍｅｔ−Ｔ
ｙ ｒ−Ｇ ｌ ｎ−Ｐｒｏ−Ａｓ ｐ−Ｐｒｏ−Ｇ
］ ｕ−Ｇ Ｉ ｕ−Ｍｅｔ−Ｇ Ｉ ｕ−８ｅ ｒ−
Ａ ｒｇ−Ｔｈ ｒ−Ａ ｒｇ−Ｔｙ ｒ−Ｐｈｅ７Ｓ
ｅ ｒ−Ｐ ｒｏ−Ａ ｒｇ−１、ｅｕ Ｎ１（２
蚕だけでなく、別の昆虫からもＰＢＡＮ−Ｉと同様の脳
ペプチドが精製され、幅広い昆虫種に対してフェロモジ
誘導活性が確認されている（Ａ、に、ｌ？ａｎｊａ、ｅ
ｔ、ａｌ、、５ＣＩＥＮＣＥ、ＶＯｌ、２４４，１９．
Ｍａｙ。H-Leu-8e r-G I u-As p-Mei
-Pro-A I
a-As p-G I n-G I u-Met-T
y r-G l n-Pro-As p-Pro-G
] u-G I u-Met-G I u-8e r-
A rg-Th r-A rg-Tyr-Phe7S
e r-Pro-A rg-1, eu N1 (2 Brain peptides similar to PBAN-I have been purified not only from silkworms but also from other insects, and their pheromodi-inducing activity has been confirmed against a wide range of insect species. There is (A, ni, l?anja, e
t,al,,5CIENCE,VOl,244,19.
May.
１９８９、Ｐ７９８〜７９８）。1989, P798-798).
しかし、ＰＢＡＮ−Ｉ等の生理活性物質は、−般に比活
性が高く、不純物の影響を受けやすい。However, physiologically active substances such as PBAN-I generally have high specific activity and are easily affected by impurities.
天然型ＰＢＡＮ−１は、３３残基の長いペプチドからな
るため、高純度のＰＢＡＮ−Ｉを大量に化学合成するこ
とは困難である。Since natural PBAN-1 consists of a long peptide of 33 residues, it is difficult to chemically synthesize a large amount of highly purified PBAN-I.
本発明は、かかる点に鑑みてなされたものであり、化学
的に大量にかつ高純度で合成することができる昆虫フェ
ロモン生合成誘導活性を有する新 ゛規ペプチドを提供
するものである。The present invention has been made in view of the above, and provides a novel peptide having insect pheromone biosynthesis-inducing activity that can be chemically synthesized in large quantities and with high purity.
上記課題を解決するために、本発明者は、容易に合成及
び精製を行うことができる簡単な構造からなる新規ペプ
チドを得ることを目的として、天然型ＰＢＡＮ−Ｉの３
３の残基のうち、昆虫性フエロモンの生合成誘導活性に
直接関与するアミノ酸残基の特定を試みた。その結果、
ＰＢＡＮ−１の部分構造をもつ合成修飾ペプチド及びそ
れらの誘導体からなる新規ペプチドを見出した。In order to solve the above problems, the present inventor aimed to obtain a novel peptide consisting of a simple structure that can be easily synthesized and purified.
Among the three residues, we attempted to identify the amino acid residues that are directly involved in the biosynthesis-inducing activity of insect pheromone. the result,
We have discovered novel peptides consisting of synthetic modified peptides having a partial structure of PBAN-1 and their derivatives.
すなわち、本発明は、
一般式（Ｉ）：
Ｒ−Ｐｈ’ｅ−Ｘ １−Ｐｒｏ−Ａｒｇ−Ｌｅｕ−ＮＨ
２（式中、Ｒは、Ｈ＋ アセチル基またはベンゾイル基
を示す。Ｘｌは、Ｓｅｒ、Ｔｈｒ、Ａｌａ、Ｐｒｏまた
はＶ’ａ ｌを示す。）
で表されるペプチドである。That is, the present invention provides general formula (I): R-Ph'e-X 1-Pro-Arg-Leu-NH
2 (wherein R represents an H+ acetyl group or a benzoyl group; Xl represents Ser, Thr, Ala, Pro or V'al).
また、本発明は、一般式（ＩＩ）：
Ｒ−（Ｘ ２ ） ｎ −Ｐｈｅ−Ｘ 、−Ｐｒｏ−Ａ
ｒｇ−Ｌｅｕ−ＮＨ２（゛式中、Ｒは、Ｈｌ アセチル
基またはベンゾイル基を示す。Ｘ、は、Ｓｅｒ、Ｔｈｒ
、Ａｌａ、ＰｒｏまたはＶａｌを示す。Ｘ２は、一般的
なアミノ酸を示す。ｎは、１〜４の整数を示す。）
で表されるペプチドである。The present invention also provides general formula (II): R-(X2)n-Phe-X, -Pro-A
rg-Leu-NH2 (in the formula, R represents Hl acetyl group or benzoyl group; X represents Ser, Thr
, Ala, Pro or Val. X2 represents a common amino acid. n represents an integer of 1 to 4. ) is a peptide represented by
〔実施例〕 以下、本発明の実施例について詳細に説明する。〔Example〕 Examples of the present invention will be described in detail below.
本発明に係る新規ペプチドである合成修飾ペプチドは、
Ｆｍｏ ｃ法（国産化学社製のペプチド合成キット）ま
たは、゛全自動ペプチド合成機（アプライドバイオシス
テムズ社製のＡＢＩモデル４３０Ａ）を用いたｔＢ ｏ
ｃ法により固相法で合成した。また、アミノ末端のア
セチル化及びベンゾイル化は、レジンと保護基を脱離し
た後、無水酢酸、塩化ベンゾイルと反応させることによ
り行った。The synthetically modified peptide, which is a novel peptide according to the present invention, is
Fmoc method (peptide synthesis kit manufactured by Kokusan Kagaku Co., Ltd.) or tBo using a fully automatic peptide synthesizer (ABI model 430A manufactured by Applied Biosystems).
It was synthesized by solid phase method using c method. Furthermore, acetylation and benzoylation of the amino terminal were performed by removing the resin and the protecting group and then reacting with acetic anhydride and benzoyl chloride.
このようにして得られた合成ペプチドを、逆相高速液体
クロマトグラフィー［装置、島津ＬＣ−６Ａ、カラム；
センシュウカガク０ＤＳ−Ｈ−１２５１，４，６Ｘ２５
０ｍｎ＋、溶媒；０．１％トリフルオロ酢酸水溶液０〜
３０％ＣＨ３ＣＮ、流速１ｎΩ／分］により精製した。The thus obtained synthetic peptide was subjected to reverse phase high performance liquid chromatography [equipment, Shimadzu LC-6A, column;
Senshu Kagaku 0DS-H-1251, 4, 6X25
0mn+, solvent; 0.1% trifluoroacetic acid aqueous solution 0~
30% CH3CN, flow rate 1 nΩ/min].
［昆虫フェロモン生合成誘導活性の測定コ本発明の新規
ペプチドの昆虫フェロモン生合成誘導活性を、蚕を用い
た生物検定により測定した。[Measurement of insect pheromone biosynthesis-inducing activity] The insect pheromone biosynthesis-inducing activity of the novel peptide of the present invention was measured by a bioassay using silkworms.
生物検定に使用した蚕は、Ｃ１４０（雌）とＪ１４０（
雄）のＦ１ハイブリッドである。このハイブリッド系は
、雄のほうがやや白っぽいため、容易に雌雄を判別でき
る。このハイブリッド系の幼虫を、成用の半人工餌（ヤ
クルト社製）により、２５℃、４時間ごとに明暗を切り
替える条件下で、１６時間飼育した。雌の蜘のうち１．
９±０．２ｇのものを選び出して以下の試験に使用した
。The silkworms used for the bioassay were C140 (female) and J140 (
It is an F1 hybrid of male). Males of this hybrid type are slightly whitish, making it easy to tell the sexes apart. These hybrid larvae were reared for 16 hours at 25° C. with light and darkness switched every 4 hours using semi-artificial adult food (manufactured by Yakult). 1 of the female spiders.
A sample weighing 9±0.2 g was selected and used in the following test.
羽化後２時間を経過した成虫を断頭した後、各種濃度の
検定用試料１．０ｇｇをマイクロシリンジで注射した。After decapitating the adults 2 hours after emergence, 1.0 gg of test samples at various concentrations were injected with a microsyringe.
注射後３時間の成虫の腹部からホルモン腺を摘出した。Hormone glands were excised from the abdomens of adult worms 3 hours after injection.
摘出したホルモン腺を酢酸エチルで抽出した。この抽出
物を高速液体クロマトグラフィー［装置；島原ＬＣ−６
Ａ、カラムＮｕｅｌｅｏｃｉｌ ５０ＤＳ （８ｍｍ
ｉ、ｄ、 Ｘ １５ｃｍ） 、溶媒；メタノール：水＝
９３ニア、流速１．５ｍｌ／分］により蚕のフェロモン
であるボンビコールを定量した。The removed hormone glands were extracted with ethyl acetate. This extract was subjected to high performance liquid chromatography [equipment: Shimabara LC-6
A, Column Nueleocil 50DS (8mm
i, d, X 15cm), solvent; methanol: water =
93nia, flow rate 1.5 ml/min], bombycol, a silkworm pheromone, was quantified.
フェロモン生合成誘導活性は、検体生物の固体差が大き
いため、検定用試料のかわりにＰＢＡＮ−１を注射した
コントロールのボンビコール生成量を（＋＋）として、
ボンビコールのピークが全く得られないものを（−）、
ボンビコールの存在が僅かに認められるものを（±）、
コントロールに比べて略半分量のボンビコールを生成す
るものを（＋）として評価した。Since the pheromone biosynthesis induction activity varies greatly among sample organisms, the amount of bombycol produced in a control in which PBAN-1 was injected instead of the test sample was set as (++).
Those in which no peak of bombycol was obtained (−),
Those in which the presence of bombykol is slightly recognized (±),
Those that produced approximately half the amount of bombycol compared to the control were evaluated as (+).
上述の生物検定方法に従って、本発明に係る修飾ペプチ
ドの実施例及び比較例についてフェロモン生合成誘導活
性を検定した結果を、下記表１に示す。Table 1 below shows the results of testing the pheromone biosynthesis inducing activity of the modified peptides according to the present invention in Examples and Comparative Examples according to the above bioassay method.
表１から明らかなように、検定用試料Ｎｏ、２〜７の５
〜１０個のアミノ酸残基からなる本発明に係る合成修飾
ペプチドは、１ ｎｍｏｌの試料濃度では、いずれも天
然型のＰＢＡＮ−Ｉと同等のフェロモン生合成誘導活性
を示した。特に、検定用試料Ｎｏ、４〜７の合成修飾ペ
プチドは、１００ｐＨＩＯ＋の試料濃度においても、Ｐ
ＢＡＮ−Ｉと同等のフェロモン生合成誘導活性を示した
。As is clear from Table 1, test sample No. 5 of 2 to 7
At a sample concentration of 1 nmol, all of the synthetically modified peptides according to the present invention consisting of ~10 amino acid residues exhibited pheromone biosynthesis-inducing activity equivalent to that of natural PBAN-I. In particular, the synthetically modified peptides of test sample Nos. 4 to 7 showed P
It showed pheromone biosynthesis inducing activity equivalent to BAN-I.
これに対して、検定用試料Ｎｏ、１及び１２の４個のア
ミノ酸残基からなる比較例の合成修飾ペプチドは、ボン
ビコールの分泌が殆ど見られず、フェロモン生合成誘導
活性を示さなかった。On the other hand, the comparative synthetically modified peptides consisting of four amino acid residues of assay samples No. 1 and 12 showed almost no secretion of bombykol and did not exhibit pheromone biosynthesis-inducing activity.
また、ペプチドのＣ末端をアミノ基で修飾していない検
定用試料Ｎｏ、８．９及び１１は、フェロモン生合成誘
導活性を示さなかった。In addition, assay samples No. 8.9 and 11, in which the C-terminus of the peptide was not modified with an amino group, did not exhibit pheromone biosynthesis-inducing activity.
また、検定用試料Ｎｏ、２の本発明に係る合成修飾ペプ
チドＨ−Ｐｈｅ−８ｅｒ−Ｐｒｏ−Ａｒｇ−Ｌｅｕ−Ｎ
ｌ２のＬｅｕのＣ末端側にＧｌｕが挿入されている検定
用試料Ｎｏ、１０は、フェロモン生合成誘導活性を示さ
なかった。In addition, the synthetic modified peptide H-Phe-8er-Pro-Arg-Leu-N according to the present invention of test sample No. 2
Assay sample No. 10, in which Glu was inserted at the C-terminal side of Leu of 12, did not show pheromone biosynthesis-inducing activity.
また、Ｃ末端から数えて６番目のＴｙｒを夫々Ｐｈｅ
、 Ｌｅｕ 、 Ａ ｌ ａに代えた検定用試料Ｎｏ、
１３〜１５の６個のアミノ酸残基からなる合成修飾ペプ
チドは、いずれもｌｎｍｏｌの試料濃度においてＰＢＡ
Ｎ−Ｉと同等のフェロモン生合成誘導活性を示した。In addition, the 6th Tyr counting from the C-terminus was
, Leu, and testing sample No. in place of Al a.
Synthetic modified peptides consisting of 6 amino acid residues 13 to 15 were all synthesized by PBA at a sample concentration of lnmol.
It showed pheromone biosynthesis inducing activity equivalent to N-I.
また、Ｃ末端から数えて４番目のアミノ酸残基を夫々Ａ
ｌａ 、 Ｔｈｒ 、 Ｐｒｏに代えた検定用試料Ｎｏ
、１６〜１８の６個のアミノ酸残基からなる合成修飾ペ
プチドは、いずれもＩ ｎ１ｌ１０１の試料濃度におい
てＰＢＡＮ−１と同等のフェロモン生合成誘導活性を示
した。In addition, the fourth amino acid residue counting from the C-terminus is
Test sample No. in place of la, Thr, Pro
, 16 to 18, all of the synthetically modified peptides consisting of six amino acid residues exhibited pheromone biosynthesis-inducing activity equivalent to that of PBAN-1 at the sample concentration of In1l101.
また、Ｎ末端のアミノ基を夫々アセチル基、ベンゾイル
基で置換した検定用試料Ｎｏ、１９〜２２の合成修飾ペ
プチドは、いずれもＰＢＡＮ−■と同等のフェロモン生
合成誘導活性を示した。Furthermore, the synthetically modified peptides of assay samples No. 19 to 22, in which the amino group at the N-terminus was replaced with an acetyl group and a benzoyl group, respectively, showed pheromone biosynthesis inducing activity equivalent to that of PBAN-■.
以上説明した如くに、本発明の新規ペプチドは、は、化
学的に大量にかつ高純度で合成することができる。これ
により、本発明の新規ペプチドを昆虫に投与して、必要
な時期に昆虫に性フエロモンを生合成させて、害虫の誘
引捕殺に有用な昆虫性フエロモンを容易に得ることがで
きる等顕著な効果を有するものである。As explained above, the novel peptide of the present invention can be chemically synthesized in large quantities and with high purity. As a result, remarkable effects such as the ability to easily obtain insect pheromone useful for attracting and killing pests by administering the novel peptide of the present invention to insects and causing the insects to biosynthesize sex pheromone at the required time are achieved. It has the following.
出願人代理人 弁理士 鈴江武彦
第１゛頁の続き
＠発明者国吉 久人
＠発明′者北村 昭浩
０発 明 者 安 藤 哲＠発明者中馬
達二
＠発明者島崎 利子
東京都文京区弥生１丁目１番１号 東京大学農学部農芸
化学科内
東京都文京区弥生１丁目１番１号 東京大学農学部農芸
化学科内
東京都府中市幸町３丁目５番８号 東京農工大学農学部
応用生物科学科内
神奈川県横浜市緑区梅ケ丘６番地２ 日本たばこ産業株
式％式％
神奈川県横浜市緑区梅ケ丘６番地２ 日本たばこ産業株
式会社生命科学研究所内Applicant's agent Patent attorney Takehiko Suzue Continued from page 1 @ Inventor Kuniyoshi Hisato @ Inventor Akihiro Kitamura 0 Inventor Satoshi Ando @ Inventor Chuma
Tatsuji @ Inventor Toshiko Shimazaki 1-1-1 Yayoi, Bunkyo-ku, Tokyo 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo 3-chome Saiwaimachi, Fuchu, Tokyo No. 5-8 Tokyo University of Agriculture and Technology, Faculty of Agriculture, Department of Applied Biological Sciences, 6-2 Umegaoka, Midori-ku, Yokohama, Kanagawa Japan Tobacco Inc. 6-2 Umegaoka, Midori-ku, Yokohama, Kanagawa Prefecture Japan Tobacco Inc. Life Science Research Institute
Claims (2)
２（式中、Ｒは、Ｈ、アセチル基またはベンゾイル基を
示す。Ｘ＿１は、Ｓｅｒ、Ｔｈｒ、Ａｌａ、Ｐｒｏまた
はＶａｌを示す。） で表されるペプチド。(1) General formula (I): R-Phe-X_1-Pro-Arg-Leu-NH_
2 (wherein, R represents H, an acetyl group, or a benzoyl group; X_1 represents Ser, Thr, Ala, Pro, or Val).
−Ｌｅｕ−ＮＨ＿２（式中、Ｒは、Ｈ、アセチル基また
はベンゾイル基を示す。Ｘ＿１は、Ｓｅｒ、Ｔｈｒ、Ａ
ｌａ、ＰｒｏまたはＶａｌを示す。Ｘ＿２は、一般的な
アミノ酸を示す。ｎは、１〜４の整数を示す。） で表されるペプチド。(2) General formula (II): R-(X_2)_n-Phe-X_1-Pro-Arg
-Leu-NH_2 (wherein, R represents H, an acetyl group, or a benzoyl group; X_1 represents Ser, Thr, A
Indicates la, Pro or Val. X_2 represents a common amino acid. n represents an integer of 1 to 4. ) Peptide represented by.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2338643A JPH04208300A (en) | 1990-11-30 | 1990-11-30 | New peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2338643A JPH04208300A (en) | 1990-11-30 | 1990-11-30 | New peptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH04208300A true JPH04208300A (en) | 1992-07-29 |
Family
ID=18320106
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2338643A Pending JPH04208300A (en) | 1990-11-30 | 1990-11-30 | New peptide |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH04208300A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995029191A1 (en) * | 1994-04-24 | 1995-11-02 | State Of Israel | Peptide fragments and analogs derived from pban 1-33 nh2 for controlling moths |
| WO2015052701A1 (en) | 2013-10-07 | 2015-04-16 | The State Of Israel, Ministry Of Agriculture & Rural Development, Agricultural Research Organization (Aro), (Volcani Center) | Novel neuropeptides useful as insecticides |
-
1990
- 1990-11-30 JP JP2338643A patent/JPH04208300A/en active Pending
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995029191A1 (en) * | 1994-04-24 | 1995-11-02 | State Of Israel | Peptide fragments and analogs derived from pban 1-33 nh2 for controlling moths |
| US6358927B1 (en) | 1994-04-24 | 2002-03-19 | State Of Israel | Peptide fragments and analogs derived from PBAN 1-33 NH2 for controlling moths |
| WO2015052701A1 (en) | 2013-10-07 | 2015-04-16 | The State Of Israel, Ministry Of Agriculture & Rural Development, Agricultural Research Organization (Aro), (Volcani Center) | Novel neuropeptides useful as insecticides |
| US9951110B2 (en) | 2013-10-07 | 2018-04-24 | The State of Israel Agriculture Research Org | Neuropeptides useful as insecticides |
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