Genetically Encoded Peptide-protein Reactive Pairs

Jing Fang; Wen-bin Zhang

doi:10.11777/j.issn1000-3304.2018.18034

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Genetically Encoded Peptide-protein Reactive Pairs

Feature Articles | 更新时间：2021-01-26

- Genetically Encoded Peptide-protein Reactive Pairs
- Acta Polymerica Sinica Issue 4, Pages: 429-444(2018)
- 作者机构：
  
  高分子化学与物理教育部重点实验室软物质科学与工程中心北京大学化学与分子工程学院北京 100871
- 作者简介：
- 基金信息：
- DOI：10.11777/j.issn1000-3304.2018.18034
  CLC：
- Published：20 April 2018，
  
  Received：1 February 2018，
  
  Revised：22 February 2018，
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Jing Fang, Wen-bin Zhang. Genetically Encoded Peptide-protein Reactive Pairs. [J]. Acta Polymerica Sinica (4):429-444(2018)
DOI：

Jing Fang, Wen-bin Zhang. Genetically Encoded Peptide-protein Reactive Pairs. [J]. Acta Polymerica Sinica (4):429-444(2018) DOI： 10.11777/j.issn1000-3304.2018.18034.

摘要

蛋白质的化学修饰在蛋白质工程、生物材料以及化学生物学等领域具有重要的意义.近年来，可基因编码的多肽-蛋白质化学反应对的发展为蛋白质的化学修饰提供了新的思路和强大的工具.本专论回顾了此类新型化学方法的发展背景，详细阐述了多肽-蛋白质反应对的作用原理和调控机制，介绍了业内在拓展一大类具有各种特性的反应对家族方面的初步尝试，并总结了它们在蛋白质拓扑工程学、蛋白质材料以及蛋白纳米组装体等诸多方面的应用.蛋白质独特的可基因编码的特性赋予了其广泛的可修饰性和体内应用的潜力，而由其衍生的诸多蛋白质超分子结构更为发展人工蛋白质机器以及多功能的"活"材料奠定了基础.

Abstract

Chemical modification of proteins is of great significance in protein engineering

biomaterials

and chemical biology. Genetically encoded peptide-protein reactive pair

or "molecular superglue"

refers to a peptide tag and its protein partner that can spontaneously reconstitute to form an isopeptide or ester bond between the side chains of specific residues of the two components. It is entirely based on natural amino acids and thus genetically encodable

providing a new way to do chemistry with proteins. This feature article summarizes the development of this unique set of chemical tools and elaborates on the principles and mechanisms of the isopeptide formation as well as the application of these tools in diverse fields. To date

a toolbox of peptide-protein reactive pairs has been developed and gradually gained its popularity in various fields such as protein topology engineering

protein-based biomaterials and protein nano-assemblies. Typical pairs include the isopeptide-bond-forming SpyTag/SpyCatcher

SnoopTag/SnoopCatcher

SdyTag/SdyCatcher

etc

. and the ester-bond-forming Cpe0147-A/Cpe0147-B. It allows the programming of post-translational modification of nascent proteins

in vivo

which

in combination with protein folding

leads to versatile nonlinear protein topologies with unique properties

including circular proteins

star proteins

and protein catenanes. The protein catenation is found to enhance both the stability and the activity of the enzyme like dihydrofolate reductase. Their reactivity

in vitro

is also excellent. The covalent nature of SpyTag/SpyCatcher interaction has facilitated the processing of proteins into various materials forms including all-protein-based

chemically cross-linked hydrogels

functional layer-by-layer thin films

hybrid colloidal assemblies

and "living" materials. In this sense

they can serve as the "iron grip" to bring two parts together to form the conjugate

which may be helpful for diverse purposes such as the sortase activity enhancer. It also allows the preparation of protein nano-assemblies with ultra-high affinity

which are useful for applications like protein nanoreactors

synthetic vaccines

and protein therapeutics. The peptide-protein reactive pair technique thus opens new horizon in protein chemistry and paves the road to the synthesis and application of precision macromolecules with huge potential in real applications.

关键词

谍标签谍捕手异肽键蛋白质工程拓扑结构索烃

Keywords

SpyTagSpyCatcherIsopeptideProtein engineeringProtein topologyCatenane

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Beijing National Laboratory for Molecular Sciences, Key Laboratory of Polymer Chemistry & Physics of Ministry of Education, Center for Soft Matter Science and Engineering, College of Chemistry and Molecular Engineering, Peking University

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