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化学进展 2018, Vol. 30 Issue (8): 1121-1132 DOI: 10.7536/PC180112 前一篇   后一篇

所属专题： 酶化学

• 综述 •

基于多肽自组装的人工金属酶

王继乾*, 闫宏宇, 李洁, 张丽艳, 赵玉荣, 徐海*   

  1. 中国石油大学(华东)重质油国家重点实验室 生物工程与技术中心 青岛 266580
  • 收稿日期:2018-01-17 修回日期:2018-04-28 出版日期:2018-08-15 发布日期:2018-05-16
  • 通讯作者: 王继乾, 徐海 E-mail:jqwang@upc.edu.cn;xuh@upc.edu.cn
  • 基金资助:
    国家自然科学基金项目（No.21673293，21573287，21503275）资助
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Artificial Metalloenzymes Based on Peptide Self-Assembly

Jiqian Wang*, Hongyu Yan, Jie Li, Liyan Zhang, Yurong Zhao, Hai Xu*   

  1. State Key Laboratory of Heavy Oil Processing, Center for Bioengineering and Biotechnology, China University of Petroleum(East China), Qingdao 266580, China
  • Received:2018-01-17 Revised:2018-04-28 Online:2018-08-15 Published:2018-05-16
  • Supported by:
    This work was supported by the National Natural Science Foundation of China(No.21673293, 21573287, 21503275).
模拟酶，又称人工酶，是在分子水平上模拟天然酶活性部位的形状、大小及其微环境等结构特征的分子或分子聚集体。随着纳米科学和超分子技术的发展，构筑具有生物催化活性的超分子模拟酶已经成为科学研究和应用开发领域的热点。肽组装金属酶是以多肽分子为基本单元，在非共价作用力协同作用下形成的超分子组装体。相比其他功能性材料，肽人工金属酶的结构及生物化学性质更接近天然酶，其分子本身更利于修饰改造，且生物相容性和功能性较好，使其在模拟酶方面具有独特优势。本文总结了近年来通过多肽自组装构建人工金属酶的研究进展，重点综述了多肽组装模式、组装体微观结构、超分子结构、金属活性中心微环境以及pH值对模拟酶催化活性的影响。增加自组装微结构的稳定性、增加催化活性以及扩大由人工酶催化的反应类型是肽人工金属酶研究中的主要挑战。构筑更加稳定的肽自组装纳米结构及更加精确的活性中心以模拟天然酶的结构和活性中心是正确的策略。
关键词： 肽自组装, 模拟酶, 微观结构, 生物催化
Mimetic, or artificial enzymes are molecules or molecular aggregates that mimic the structural features of enzyme active center, such as shape, size, and microenvironment at molecular level. With the development of nanoscience and supramolecular technologies, the construction of supramolecular mimetic enzymes with specific catalytic activity has become a hotspot in both scientific research and application. Artificial peptide metalloenzymes have peptide molecules as the basic units, and the self-assembly of peptide supramolecular structure with enzymatic catalytic activity is driven by a series of non-covalent interactions synergistically. The structure and biochemical properties of peptide metalloenzyme are akin to those of natural enzymes. Furthermore, since peptide molecules are biocompatible and easy to be modified, artificial peptides metalloenzymes would be ideal candidates for artificial enzyme fabrication with specific functions. In this review, the progress of the mimetic metalloenzymes fabrication through peptide self-assembly has been summarized. The effects of peptide self-assembly, supramolecular structure, microenvironment of metal active center, as well as pH value on the artificial enzyme catalytic activity has been reviewed. The enhancement of the stability of self-assembled nanostructures, the improvement of catalytic activity and the broadening of the reaction types catalyzed by artificial enzymes are the main challenge in artificial peptides metalloenzyme study. Fabrication more stable peptide self-assembled nanostructure and more precise active centers to mimic those of the natural enzymes might be the right strategies.
Contents
1 Introduction
2 Effects of self-assembly nanostructures on metalloenzyme
2.1 Nanotube
2.2 Nanofibers
2.3 Coiled-coil
3 The secondary structure of peptide self-assemblies in metalloenzyme
3.1 β-hairpin
3.2 α-helix
4 Effects of spatial structure on metalloenzyme
4.1 Regulation of metal ions
4.2 Formation of protein interface
4.3 Hydrophobic interface
5 Metal-free peptide self-assembly artificial enzyme
6 Conclusion and outlook
Key words: peptide self-assembly, mimetic enzyme, microstructure, biocatalysis

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[1] Bairoch A. Nucleic Acids Res., 2000, 28:304.
[2] Young D D, Nichols J, Kelly R M, Deiters A. J. Am. Chem. Soc., 2008, 130:10048.
[3] 刘盛华(Liu J J), 吴成泰(Wu C T). 化学通报(Chem.), 1998, 4:001.
[4] Paramonov S E, Jun H W, Hartgerink J D. J. Am. Chem. Soc., 2006, 128:7291.
[5] Cox E H, McLendon G L. Curr. Opin. Chem. Biol., 2000, 4:162.
[6] Wiester M J, Ulmann P A, Mirkin C A. Angew. Chem. Int. Ed., 2011, 50:114.
[7] Friedmann M P, Torbeev V, Zelenay V, Sobol A, Greenwald J, Riek R. PLoS One, 2015, 10(12):e0143948.
[8] Raynal M, Ballester P, Vidal-Ferran A, Leeuwen P W. Chem. Soc. Rev., 2014, 43:1734.
[9] Petrik I D, Liu J, Lu Y. Curr. Opin. Chem. Biol., 2014, 19:67.
[10] Shen X F, Deng X R, Pang Y H. RSC Adv., 2014, 4:21840.
[11] Dublin S N, Conticello V P. J. Am. Chem. Soc., 2008, 130:49.
[12] Dong J J, Canfield J M, Mehta A K, Shokes J E, Tian B,Childers W S,Simmons J A, Mao Z X, Scott R A, Warncke K, Lynn D G. Proc. Natl. Acad. Sci.U.S.A., 2007, 104:13313.
[13] Ayton S, Lei P, Bush A I. Free Radicals Biol. Med., 2013, 62:76.
[14] Lowik D W P M, Leunissen E H P, van den Heuvel M, Hansen M B, van Hest J C M. Chem. Soc. Rev., 2010, 39:3394.
[15] Yang Z H, Zhao X J. Int. J. Nanomed., 2011, 6:303.
[16] Ravichandran R, Venugopal J R, Sundarrajan S, Mukherjee S, Ramakrishna S. Biomaterials, 2012, 33:846.
[17] Cui H G, Cheetham A G, Pashuck E T, Stupp S I. J. Am. Chem. Soc., 2014, 136:12461.
[18] Pedersen C J. J. Am. Chem. Soc., 1967, 89:7017.
[19] Cram D J. J. Inclusion Phenom., 1988, 6:397.
[20] Lehn J M. J. Inclusion Phenom., 1988, 6:351.
[21] Sherrington D C, Taskinen K A. Chem. Soc. Rev., 2001, 30:83.
[22] Yu S J, Huang X, Miao L, Zhu J Y, Yin Y Z, Luo Q, Xu J Y, Shen J C, Liu J Q. Bioorg. Chem., 2010, 38:159.
[23] Whitesides G M, Grzybowski B. Science, 2002, 295:2418.
[24] Maeda Y, Makhlynets O V, Matsui H, Korendovych I V. Annu. Rev. Biomed. Eng., 2016, 18:311.
[25] Jin Q X, Zhang L, Cao H, Wang T Y, Zhu X F, Jiang J, Liu M H. Langmuir, 2011, 27:13847.
[26] Tena-Solsona M, Nanda J, Chotera A, Ashkenasy G, Escuder B. Chem. Eur. J., 2016, 22:6687.
[27] Huang Z P, Luo Q, Guan S W, Gao J X, Wang Y G, Zhang B, Wang L, Xu J Y, Dong Z Y, Liu J Q. Soft Matter, 2014, 10:9695.
[28] Omosun T O, Hsieh M C, Childers W S, Das D, Mehta A K, Anthony N R, Pan T, Grover M A, Berland K M, Lynn D G. Nat. Chem., 2017, 9:805.
[29] Rufo C M, Moroz Y S, Moroz O V, Stohr J, Smith T A, Hu X, DeGrado W F, Korendovych I V. Nat. Chem., 2014, 6:303.
[30] Lee M W, Wang T, Makhlynets O V, Wu Y B, Polizzi N F, Wu H F, Gosavi P M, Stohr J, Korendovych I V, DeGrado W F, Hong M. Proc. Natl. Acad. Sci.U.S.A., 2017, 114:6191.
[31] Singh N, Conte M P, Ulijn R V, Miravet J F, Escuder B. Chem. Commun., 2015, 51(67):13213.
[32] Guler M O, Stupp S I. J. Am. Chem. Soc., 2007, 129:12082.
[33] Zhang C Q, Xue X D, Luo Q, Li Y W, Yang K N, Zhuang X X, Jiang Y G, Zhang J C, Liu J Q, Zou G Z, Liang X J. ACS Nano, 2014, 8:11715.
[34] Landschulz W H, Johnson P F, McKnight S L. Science, 1988, 240:1759.
[35] Zastrow M L, Pecoraro V L. J. Am. Chem. Soc., 2013, 135:5895.
[36] Cangelosi V M, Deb A, Penner-Hahn J E, Pecoraro V L. Angew. Chem. Int. Ed., 2014, 53:7900.
[37] Burton A J, Thomson A R, Dawson W M, Brady R L, Woolfson D N. Nat. Chem., 2016, 8:837.
[38] Pochan D J, Schneider J P, Kretsinger J, Ozbas B, Rajagopal K, Haines L. J. Am. Chem. Soc., 2003, 125:11802.
[39] Micklitsch C M, Medina S H, Yucel T, Nagy-Smith K J, Pochan D J, Schneider J P. Macromolecules, 2015, 48:1281.
[40] Rughani R V, Schneider J P. MRS Bull., 2008, 33:530.
[41] Knerr P J, Branco M C, Nagarkar R, Pochan D J, Schneider J P. J. Mater. Chem., 2012, 22:1352.
[42] Micklitsch C M, Knerr P J, Branco M C, Nagarkar R, Pochan D J, Schneider J P. Angew. Chem. Int. Ed., 2011, 50:1577.
[43] Platt G, Chung C W, Searle M S. Chem. Commun., 2001,13(13):1162.
[44] Wang C, Sun Y, Wang J, Xu H, Lu J. R. Chem. Asian J., 2015, 10:1953.
[45] Rajagopal K, Lamm M S, Haines-Butterick L A, Pochan D J, Schneider J P. Biomacromolecules, 2009, 10:2619.
[46] Schneider J P, Pochan D J, Ozbas B, Rajagopal K, Pakstis L, Kretsinger J. J. Am. Chem. Soc., 2002, 124:15030.
[47] Tanaka T, Mizuno T, Fukui S, Hiroaki H, Oku J, Kanaori K, Tajima K, Shirakawa M. J. Am. Chem. Soc.,2004, 126:14023.
[48] Kharenko O A, Ogawa M Y. J. Inorg. Biochem., 2004, 98:1971.
[49] Cerasoli E, Sharpe B K, Woolfson D N. J. Am. Chem. Soc., 2005, 127:15008.
[50] Banwell E F, Abelardo E S, Adams D J, Birchall M A, Corrigan A, Donald A M, Kirkland M, Serpell L C, Butler M F, Woolfson D N. Nat. Mater., 2009, 8:596.
[51] Gao Y, Zhao F, Wang Q G, Zhang Y, Xu B. Chem. Soc. Rev., 2010, 39:3425.
[52] Valéry C, Deville-Foillard S, Lefebvre C, Taberner N, Legrand P, Meneau F, Meriadec C, Delvaux C, Bizien T, Kasotakis E, Lopez-Iglesias C, Gall A, Bressanelli S, Du M L, Paternostre M, Artzner F. Nat. Commun., 2015, 6:7771.
[53] Castelletto V, Hamley I W, Segarra-Maset M D, Gumbau C B, Miravet J F, Escuder B, Seitsonen J, Ruokolainen J. Biomacromolecules, 2014, 15:591.
[54] Wang J, Shao F, Li W, Yan J, Liu K, Tao P, Masuda O, Zhang A. Chem. Asian J., 2017, 12:497.
[55] Zastrow M L, Peacock A F, Stuckey J A, Pecoraro V L. Nat. Chem., 2011, 4:118.
[56] Der B S, Edwards D R, Kuhlman B. Biochemistry, 2012, 51:3933.
[57] Song W J, Tezcan F A. Science, 2014, 346:1525.
[58] Broo K S, Brive L, Ahlberg P, Baltzer A L. J. Am. Chem. Soc., 1997, 119:11362.
[59] Hiebler K, Lengyel Z, Castaneda C A, Makhlynets O V. Proteins, 2017, 85:1656.
[60] Sun Y, Zhao C, Gao N, Ren J, Qu X. Chem. Eur. J., 2017, 23(71):18146.
[61] Garcia A M, Kurbasic M, Kralj S, Melchionna M, Marchesan S. Chem. Commun., 2017, 53(58):8110.
[62] Huang Z P, Guan S W, Wang Y G, Shi G N, Cao L N, Gao Y Z, Dong Z Y, Xu J Y, Luo Q, Liu J Q. J. Mater. Chem. B, 2013, 1:2297.
[63] Zhang C Q, Shafi R, Lampel A, MacPherson D, Pappas C G, Narang V, Wang T, Maldarelli C, Ulijn R V. Angew. Chem. Int. Ed., 2017, 56:14511.
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摘要

基于多肽自组装的人工金属酶