Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid flowers

Zijian Zhao; Ji Zhang; Mingyang Wang; Zhi Wang; Liping Wang; Li Ma; Xuri Huang; Zhengqiang Li

doi:10.1039/c6ra24192a

Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid flowers

Zijian Zhao, Ji Zhang, Mingyang Wang, Zhi Wang, Liping Wang, Li Ma, Xuri Huang, Zhengqiang Li

Biochemistry, Chemistry, & Physics

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

This work reports a facile method for hybridizing deuterohemin-peptide (DhHP-6) with copper phosphate to form deuterohemin-peptide-inorganic hybrid flowers (DhHP-6-Cu₃(PO₄)₂) by self-assembly. The DhHP-6-Cu₃(PO₄)₂ flowers have been characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and solid state UV-vis. In the assembly process, the DhHP-6 peptides are fixed on Cu₃(PO₄)₂ through the coordination of the end amino acids (Lys6) with copper(ii) centers. The rearrangement of Lys6 prevents DhHP-6 aggregation. Hence, DhHP-6-Cu₃(PO₄)₂ flowers exhibit a nearly 300% enhancement of peroxidase-like activity in comparison with free DhHP-6 in solution. Meanwhile, the DhHP-6-Cu₃(PO₄)₂ flowers show stronger affinity towards 3,3,5,5-tetramethylbenzidine (TMB) and H₂O₂ than free DhHP-6 and horseradish peroxidase (HRP). In addition, EPR results provide direct evidences for the mechanisms of DhHP-6-Cu₃(PO₄)₂ flower growth and activity enhancement. Furthermore, the sample presents excellent reusability and storage stability.

Original language	English
Pages (from-to)	104265-104272
Number of pages	8
Journal	RSC Advances
Volume	6
Issue number	106
DOIs	https://doi.org/10.1039/c6ra24192a
State	Published - 2016

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title = "Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid flowers",

abstract = "This work reports a facile method for hybridizing deuterohemin-peptide (DhHP-6) with copper phosphate to form deuterohemin-peptide-inorganic hybrid flowers (DhHP-6-Cu3(PO4)2) by self-assembly. The DhHP-6-Cu3(PO4)2 flowers have been characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and solid state UV-vis. In the assembly process, the DhHP-6 peptides are fixed on Cu3(PO4)2 through the coordination of the end amino acids (Lys6) with copper(ii) centers. The rearrangement of Lys6 prevents DhHP-6 aggregation. Hence, DhHP-6-Cu3(PO4)2 flowers exhibit a nearly 300% enhancement of peroxidase-like activity in comparison with free DhHP-6 in solution. Meanwhile, the DhHP-6-Cu3(PO4)2 flowers show stronger affinity towards 3,3,5,5-tetramethylbenzidine (TMB) and H2O2 than free DhHP-6 and horseradish peroxidase (HRP). In addition, EPR results provide direct evidences for the mechanisms of DhHP-6-Cu3(PO4)2 flower growth and activity enhancement. Furthermore, the sample presents excellent reusability and storage stability.",

author = "Zijian Zhao and Ji Zhang and Mingyang Wang and Zhi Wang and Liping Wang and Li Ma and Xuri Huang and Zhengqiang Li",

note = "Publisher Copyright: {\textcopyright} 2016 The Royal Society of Chemistry.",

year = "2016",

doi = "10.1039/c6ra24192a",

language = "English",

volume = "6",

pages = "104265--104272",

journal = "RSC Advances",

issn = "2046-2069",

publisher = "Royal Society of Chemistry",

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T1 - Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid flowers

AU - Zhao, Zijian

AU - Zhang, Ji

AU - Wang, Mingyang

AU - Wang, Zhi

AU - Wang, Liping

AU - Ma, Li

AU - Huang, Xuri

AU - Li, Zhengqiang

PY - 2016

Y1 - 2016

N2 - This work reports a facile method for hybridizing deuterohemin-peptide (DhHP-6) with copper phosphate to form deuterohemin-peptide-inorganic hybrid flowers (DhHP-6-Cu3(PO4)2) by self-assembly. The DhHP-6-Cu3(PO4)2 flowers have been characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and solid state UV-vis. In the assembly process, the DhHP-6 peptides are fixed on Cu3(PO4)2 through the coordination of the end amino acids (Lys6) with copper(ii) centers. The rearrangement of Lys6 prevents DhHP-6 aggregation. Hence, DhHP-6-Cu3(PO4)2 flowers exhibit a nearly 300% enhancement of peroxidase-like activity in comparison with free DhHP-6 in solution. Meanwhile, the DhHP-6-Cu3(PO4)2 flowers show stronger affinity towards 3,3,5,5-tetramethylbenzidine (TMB) and H2O2 than free DhHP-6 and horseradish peroxidase (HRP). In addition, EPR results provide direct evidences for the mechanisms of DhHP-6-Cu3(PO4)2 flower growth and activity enhancement. Furthermore, the sample presents excellent reusability and storage stability.

AB - This work reports a facile method for hybridizing deuterohemin-peptide (DhHP-6) with copper phosphate to form deuterohemin-peptide-inorganic hybrid flowers (DhHP-6-Cu3(PO4)2) by self-assembly. The DhHP-6-Cu3(PO4)2 flowers have been characterized by scanning electron microscopy, Fourier transform infrared spectroscopy and solid state UV-vis. In the assembly process, the DhHP-6 peptides are fixed on Cu3(PO4)2 through the coordination of the end amino acids (Lys6) with copper(ii) centers. The rearrangement of Lys6 prevents DhHP-6 aggregation. Hence, DhHP-6-Cu3(PO4)2 flowers exhibit a nearly 300% enhancement of peroxidase-like activity in comparison with free DhHP-6 in solution. Meanwhile, the DhHP-6-Cu3(PO4)2 flowers show stronger affinity towards 3,3,5,5-tetramethylbenzidine (TMB) and H2O2 than free DhHP-6 and horseradish peroxidase (HRP). In addition, EPR results provide direct evidences for the mechanisms of DhHP-6-Cu3(PO4)2 flower growth and activity enhancement. Furthermore, the sample presents excellent reusability and storage stability.

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U2 - 10.1039/c6ra24192a

DO - 10.1039/c6ra24192a

M3 - Article

AN - SCOPUS:84994434574

SN - 2046-2069

VL - 6

SP - 104265

EP - 104272

JO - RSC Advances

JF - RSC Advances

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ER -

Structure advantage and peroxidase activity enhancement of deuterohemin-peptide-inorganic hybrid flowers

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