Insect Diapause, its Chemical Control and Elucidation of Molecular Mechanism

昆虫滞育、化学防治及分子机制的阐明

• 批准号: 04453138
• 负责人: ISOBE Minoru
• 金额: $ 4.22万
• 依托单位: Nagoya University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (B)
• 财政年份: 1992
• 资助国家: 日本
• 起止时间: 1992 至 1993
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-04453138/
• 关键词: diapause hormone; peptide; amidated C-termunal peptide; hydrophobicity; HPLC; silkworm, Bombyx mori; structure relationship

To determine the structure-activity relationships of diapause hormone of the silkworm, Bombyx mori, a series of peptide analogs having different chain length starting from the parent C-termunus an analogs having free acid C-terminal were chemically synthesized by solid-phase Fmoc methodology and were further purified by HPLC.Bioassay elicited the non-active nature of the free acid C-termunus and the retained activity of those shorter chain with the amidated C-termunal analogs among which the response depended on the length of the chain. It means that the active peptides required two minimal elements, namely the sequence near and the amidation of the C-termunus. The amidated C-termunus did not show better protective role against enzymatic digestion in pupal and larval haemolymph than the free acid C-termunal analog. This suggested its involvement in the existence of a certain higher order structure needed in expression of biological activity. Moreover, as most of the hydrophobic amino acids locate close to the C-termunal portion, the sequence near that terminus could be alternatively related to the necessary hydrophobicity. Consequently, both the hydrophobicity of the portion near and the amidation of the C-termunus were indispensable structure for diapause hormone activity.

To determine the structure-activity relationships of diapause hormone of the silkworm, Bombyx mori, a series of peptide analogs having different chain length starting from the parent C-termunus an analogs having free acid C-terminal were chemically synthesized by solid-phase Fmoc methodology and were further purified by HPLC.Bioassay elicited the non-active nature of the free acid C-termunus and the retained activity of those较短的链带有氨基化的c术语类似物，其中响应取决于链的长度。这意味着活性肽需要两个最小元素，即附近的序列和c-termunus的亚。与游离的酸C-术语类似物相比，胺化的c-术语没有在pupal和幼虫血液中表现出更好的保护作用。这表明它参与了生物活性表达所需的一定高阶结构。此外，由于大多数疏水性氨基酸都位于C-Termunal部分附近，因此该末端附近的序列可能与必要的疏水性相关。因此，附近部分的疏水性和c-termunus的肿瘤都是育间激素活性的必不可少的结构。

项目成果

Isobe,M.: "Silkworm Diapause Hormone,Structure-Activity Relationships-----Indispensable Role of C-Terminal Amide." J.Insect Biochemistry and Molecular Biology.(in Press).

Isobe,M.：“家蚕滞育激素，结构-活性关系——C端酰胺的不可或缺的作用。”

Sato, Y.: "Precursor Polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori : Characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides." Proc.Natl.

Sato, Y.：“家蚕食管下神经节分泌的多种神经肽的前体多蛋白：编码滞育激素前体的 cDNA 的表征和其他肽的鉴定。”

Yukihiro Sato: "A New Diapause Hormone Molecule of the Silkworm,Bombyx mori" Proceedings of the Japan Academy. 68. 75-79 (1992)

Yukihiro Sato：“蚕的新滞育激素分子，Bombyx mori”日本科学院院刊。

Sato,Y.: "Precursor Polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori::Characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides." Proc.Natl.Ac

Sato,Y.：“家蚕食管下神经节分泌的多种神经肽的前体多蛋白：：编码滞育激素前体的 cDNA 的表征和其他肽的鉴定。”

Isobe, M.: "Silkworm Diapause Hormone, Structure-Activity Relationships--Indispensable Role of C-Terminal Amide." J.Insect Biochemistry and Molecular Biology. (in Press).

Isobe, M.：“蚕滞育激素，结构-活性关系——C 端酰胺的不可或缺的作用。”