• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

α干扰素的蛋白质工程

Protein engineering of interferon alphas.

作者信息

Hu Renqiu, Lei Ke-Jian, Bekisz Joseph, Zoon Kathryn C

机构信息

Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institute of Health, Bethesda, MD, USA.

出版信息

Methods Mol Med. 2005;116:69-80. doi: 10.1385/1-59259-939-7:069.

DOI:10.1385/1-59259-939-7:069
PMID:16000855
Abstract

Interferon (IFN)-alphas constitute a family of proteins exhibiting high degree of homology in primary, secondary, and tertiary structure and display a high level of species specificity in their biological properties. However, small structural differences in these proteins may be responsible for a significant variety of biological actions. Understanding the structure and function of human IFN-alpha is very important. Recombinant techniques are important tools for the production and modification of IFN proteins. The first IFN hybrid, IFN-alpha1/alpha2 was constructed using recombinant technology in 1981. Subsequently, a number of IFN hybrids and mutants have been constructed, expressed and characterized. These hybrids and mutants have resulted in novel IFNs that either combine different biological properties from the parental proteins or have significantly different biological activity. Therefore, IFN hybrids and mutants have provided a powerful tool for studying the structure and function of these molecules. Also, these engineered IFNs may have important new therapeutic applications and may provide greater sights into understanding of the clinical activities of these molecules.

摘要

α干扰素(IFN-α)构成了一类蛋白质家族,它们在一级、二级和三级结构上具有高度同源性,并且在生物学特性上表现出高度的种属特异性。然而,这些蛋白质中微小的结构差异可能导致多种多样的生物学作用。了解人α干扰素的结构和功能非常重要。重组技术是生产和修饰IFN蛋白的重要工具。1981年利用重组技术构建了首个IFN杂交体,即IFN-α1/α2。随后,构建、表达并鉴定了许多IFN杂交体和突变体。这些杂交体和突变体产生了新型IFN,它们要么结合了亲本蛋白的不同生物学特性,要么具有显著不同的生物活性。因此,IFN杂交体和突变体为研究这些分子的结构和功能提供了有力工具。此外,这些经过工程改造的IFN可能具有重要的新治疗应用,并且可能为深入了解这些分子的临床活性提供更多见解。

相似文献

1
Protein engineering of interferon alphas.α干扰素的蛋白质工程
Methods Mol Med. 2005;116:69-80. doi: 10.1385/1-59259-939-7:069.
2
A structural basis for interferon-alpha-receptor interactions.干扰素-α受体相互作用的结构基础。
FASEB J. 2007 Oct;21(12):3288-96. doi: 10.1096/fj.07-8585com. Epub 2007 May 21.
3
Structure-function analysis of human IFN-alpha. Mapping of a conformational epitope by homologue scanning.人干扰素-α的结构-功能分析。通过同源扫描对构象表位进行定位。
J Immunol. 1994 Jan 15;152(2):705-15.
4
Activity of hybrid type I interferons in cells lacking Tyk2: a common region of IFN-alpha 8 induces a response, but IFN-alpha2/8 hybrids can behave like IFN-beta.缺乏酪氨酸激酶2(Tyk2)的细胞中I型杂交干扰素的活性:IFN-α8的一个共同区域可诱导反应,但IFN-α2/8杂交体的表现可能类似IFN-β。
J Interferon Cytokine Res. 2003 Nov;23(11):655-66. doi: 10.1089/107999003322558791.
5
Mutation of the IFNAR-1 receptor binding site of human IFN-alpha2 generates type I IFN competitive antagonists.人干扰素α2的IFNAR - 1受体结合位点突变产生I型干扰素竞争性拮抗剂。
Biochemistry. 2008 Nov 18;47(46):12018-27. doi: 10.1021/bi801588g. Epub 2008 Oct 21.
6
Directed evolution of gene-shuffled IFN-alpha molecules with activity profiles tailored for treatment of chronic viral diseases.通过定向进化获得基因改组的干扰素-α分子,其活性谱适合用于治疗慢性病毒性疾病。
Proc Natl Acad Sci U S A. 2007 May 15;104(20):8269-74. doi: 10.1073/pnas.0609001104. Epub 2007 May 9.
7
Human type I interferons: structure and function.人I型干扰素:结构与功能
Acta Virol. 1994 Dec;38(6):345-60.
8
The human interferon-alpha species and hybrid proteins.人α干扰素种类及杂合蛋白。
Semin Oncol. 1997 Jun;24(3 Suppl 9):S9-4-S9-17.
9
Human interferons alpha, beta and omega.人α、β和ω干扰素。
Growth Factors. 2004 Dec;22(4):243-51. doi: 10.1080/08977190400000833.
10
Human IFN-alpha protein engineering: the amino acid residues at positions 86 and 90 are important for antiproliferative activity.人干扰素α蛋白工程:86位和90位的氨基酸残基对抗增殖活性很重要。
J Immunol. 2001 Aug 1;167(3):1482-9. doi: 10.4049/jimmunol.167.3.1482.