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胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用

邓宇晨,  顾嘉伟,  聂菲,  肖良

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文章导航 > 药学实践与服务  > 2016 >  34(6): 481-484,496
邓宇晨, 顾嘉伟, 聂菲, 肖良. 胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用[J]. 药学实践与服务, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
引用本文: 邓宇晨, 顾嘉伟, 聂菲, 肖良. 胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用[J]. 药学实践与服务, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
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DENG Yuchen, GU Jiawei, NIE Fei, XIAO Liang. Cystine knot peptide's properties and its applications for drug design and molecular engineering[J]. Journal of Pharmaceutical Practice and Service, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
Citation: DENG Yuchen, GU Jiawei, NIE Fei, XIAO Liang. Cystine knot peptide's properties and its applications for drug design and molecular engineering[J]. Journal of Pharmaceutical Practice and Service, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
shu

胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用

doi: 10.3969/j.issn.1006-0111.2016.06.001
  • 1.

    第二军医大学, 海军临床医学专业学员三队, 上海 200433

  • 2.

    第二军医大学, 临床医学专业学员十一队, 上海 200433

  • 3.

    第二军医大学, 海军医学系海洋生物技术教研室, 上海 200433

基金项目: 国家自然科学基金面上项目（81470518）

Cystine knot peptide's properties and its applications for drug design and molecular engineering

  • 1.

    No. 3 Student Team, Naval Clinical Medicine, Faculty of Naval Medicine, Second Military Medical University, Shanghai 200433, China

  • 2.

    No. 11 Student Team, Clinical Medicine, Faculty of Naval Medicine, Second Military Medical University, Shanghai 200433, China

  • 3.

    Department of Marine Biotechnology, Faculty of Naval Medicine, Second Military Medical University, Shanghai 200433, China

  • 摘要: 胱氨酸结（cystine knot，CK）模体是由两对二硫键及其相连的肽链骨架形成的一个内部环以及从环中穿过的第三对二硫键组成的球形结构，广泛存在于真菌、植物、海洋软体动物、昆虫以及蜘蛛等生物的毒素多肽和蛋白质中。CK多肽结构非常稳定、生物活性多样，是一类在药物设计和分子工程研究中的理想模型分子。本文综述了抑制剂胱氨酸结（inhibitor cystine knot，ICK）多肽和环形胱氨酸结（cyclic cystine knot，CCK）多肽两类主要CK毒素的氨基酸序列、拓扑结构、排列组合、人工合成以及空间折叠等特征，并进一步阐述了其在药物设计与分子工程中的应用前景。
    Abstract: The cystine knot (CK) motif comprises an internal ring formed by two disulfide bonds and their connecting backbone segments which is threaded by a third disulfide bond. It is present in peptides and proteins of a variety of species, including fungi, plants, marine molluscs, insects and spiders. CK polypeptide is one of the ideal model molecules for drug design and molecular engineering research because of its stable structure and variety of bioactivities. Here we summarized the main structural features of both inhibitor cystine knot (ICK) peptide and cyclic cystine knot (CCK) peptide, including primary sequence, topology, permutation, synthesis and folding characteristics, as well as its applications on drug design and molecular engineering.
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出版历程
  • 收稿日期:  2015-10-30
  • 修回日期:  2016-04-26

胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用

doi: 10.3969/j.issn.1006-0111.2016.06.001
  • 1. 第二军医大学, 海军临床医学专业学员三队, 上海 200433
  • 2. 第二军医大学, 临床医学专业学员十一队, 上海 200433
  • 3. 第二军医大学, 海军医学系海洋生物技术教研室, 上海 200433
    • 基金项目:  国家自然科学基金面上项目（81470518）
  • 收稿日期: 2015-10-30
  • 修回日期: 2016-04-26

摘要: 胱氨酸结（cystine knot，CK）模体是由两对二硫键及其相连的肽链骨架形成的一个内部环以及从环中穿过的第三对二硫键组成的球形结构，广泛存在于真菌、植物、海洋软体动物、昆虫以及蜘蛛等生物的毒素多肽和蛋白质中。CK多肽结构非常稳定、生物活性多样，是一类在药物设计和分子工程研究中的理想模型分子。本文综述了抑制剂胱氨酸结（inhibitor cystine knot，ICK）多肽和环形胱氨酸结（cyclic cystine knot，CCK）多肽两类主要CK毒素的氨基酸序列、拓扑结构、排列组合、人工合成以及空间折叠等特征，并进一步阐述了其在药物设计与分子工程中的应用前景。

English Abstract

邓宇晨, 顾嘉伟, 聂菲, 肖良. 胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用[J]. 药学实践与服务, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
引用本文: 邓宇晨, 顾嘉伟, 聂菲, 肖良. 胱氨酸结模体多肽的特征及其在药物设计和分子工程中的应用[J]. 药学实践与服务, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
shu
DENG Yuchen, GU Jiawei, NIE Fei, XIAO Liang. Cystine knot peptide's properties and its applications for drug design and molecular engineering[J]. Journal of Pharmaceutical Practice and Service, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
Citation: DENG Yuchen, GU Jiawei, NIE Fei, XIAO Liang. Cystine knot peptide's properties and its applications for drug design and molecular engineering[J]. Journal of Pharmaceutical Practice and Service, 2016, 34(6): 481-484,496. doi: 10.3969/j.issn.1006-0111.2016.06.001
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