Supramolecular peptide nanotubes as artificial enzymes for catalysing ester hydrolysis

被引:3
|
作者
Song, Qiao [1 ,2 ]
Cheng, Zihe [1 ]
Perrier, Sebastien [1 ,3 ,4 ]
机构
[1] Univ Warwick, Dept Chem, Coventry CV4 7AL, W Midlands, England
[2] Southern Univ Sci & Technol, Shenzhen Grubbs Inst, Shenzhen 518055, Peoples R China
[3] Univ Warwick, Warwick Med Sch, Coventry CV4 7AL, W Midlands, England
[4] Monash Univ, Fac Pharm & Pharmaceut Sci, Parkville, Vic 3052, Australia
基金
欧洲研究理事会;
关键词
DESIGN; EFFICIENT; HYDROLASE; CATALYSIS; HYDROGEL; TRIAD;
D O I
10.1039/d3py00993a
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Peptide-based artificial enzymes are attracting significant interest because of their remarkable resemblance in both composition and structure to native enzymes. Herein, we report the construction of histidine-containing cyclic peptide-based supramolecular polymeric nanotubes to function as artificial enzymes for ester hydrolysis. The optimized catalyst shows a ca. 70-fold increase in reaction rate compared to the un-catalysed reaction when using 4-nitrophenyl acetate as a model substrate. Furthermore, the amphiphilic nature of the supramolecular catalysts enables an enhanced catalytic activity towards hydrophobic substrates. By incorporating an internal hydrophobic region within the self-assembled polymeric nanotube, we achieve a 55.4-fold acceleration in hydrolysis rate towards a more hydrophobic substrate, 4-nitrophenyl butyrate. This study introduces supramolecular peptide nanotubes as an innovative class of supramolecular scaffolds for fabricating artificial enzymes with better structural and chemical stability, catalysing not only ester hydrolysis, but also a broader spectrum of catalytic reactions. Histidine-containing cyclic peptide-based supramolecular peptide nanotubes were constructed to function as artificial enzymes for catalysing ester hydrolysis.
引用
收藏
页码:4712 / 4718
页数:7
相关论文
共 50 条
  • [41] Free extracellular enzymes dominate initial peptide hydrolysis in coastal seawater
    Liu, Shuting
    Liu, Zhanfei
    MARINE CHEMISTRY, 2018, 199 : 37 - 43
  • [42] The configuration-specialisation of a "component" esterase (the question of the natural make and artificial synthetic of the enzyme) X Announcement - Asymmetrical ester hydrolysis through enzymes
    Bamann, E
    Feichtner, C
    BIOCHEMISCHE ZEITSCHRIFT, 1936, 288 (1/2): : 70 - 78
  • [43] INFLUENCE OF SUPRAMOLECULAR AND MORPHOLOGICAL STRUCTURE OF CELLULOSE ON ITS DEGRADATION BY ENZYMES OR ACID-HYDROLYSIS
    PHILIPP, B
    JACOPIAN, V
    LOTH, F
    HIRTE, W
    SCHULZ, G
    PAPIER, 1978, 32 (12): : 538 - 545
  • [44] Rate enhancement and enantioselectivity in ester hydrolysis catalysed by cyclodextrin-peptide hybrids
    Tsutsumi, H
    Hamasaki, K
    Mihara, H
    Ueno, A
    JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, 2000, (09): : 1813 - 1818
  • [45] DIRECT CHEMICAL EVIDENCE FOR THE MIXED ANHYDRIDE INTERMEDIATE OF CARBOXYPEPTIDASE A IN ESTER AND PEPTIDE HYDROLYSIS
    SANDER, ME
    WITZEL, H
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1985, 132 (02) : 681 - 687
  • [46] The role of β-hairpin conformation in ester hydrolysis peptide catalysts based on a TrpZip scaffold
    Liu, Xinyu
    Waters, Riley
    Gilbert, Hannah E.
    Barroso, Gage T.
    Boyle, Kelsey M.
    Witus, Leah S.
    RSC ADVANCES, 2021, 11 (38) : 23714 - 23718
  • [47] Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures
    Kol, N
    Adler-Abramovich, L
    Barlam, D
    Shneck, RZ
    Gazit, E
    Rousso, I
    NANO LETTERS, 2005, 5 (07) : 1343 - 1346
  • [49] Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water
    Rho, Julia Y.
    Cox, Henry
    Mansfield, Edward D. H.
    Ellacott, Sean H.
    Peltier, Raoul
    Brendel, Johannes C.
    Hartlieb, Matthias
    Waigh, Thomas A.
    Perrier, Sebastien
    NATURE COMMUNICATIONS, 2019, 10 (1)
  • [50] Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water
    Julia Y. Rho
    Henry Cox
    Edward D. H. Mansfield
    Sean H. Ellacott
    Raoul Peltier
    Johannes C. Brendel
    Matthias Hartlieb
    Thomas A. Waigh
    Sébastien Perrier
    Nature Communications, 10