Issue 106, 2016, Issue in Progress
From the journal:

RSC Advances

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

Zijian Zhao,ab   Ji Zhang,b   Mingyang Wang,c   Zhi Wang,b   Liping Wang,c   Li Ma,*bd   Xuri Huang*a  and  Zhengqiang Li*b  

* Corresponding authors

a Institute of Theoretical Chemistry, Jilin University, Liutiao Road 2, Changchun 130023, Jilin Province, PR China
E-mail: huangxr@jlu.edu.cn

b Key Laboratory for Molecular Enzymology, Engineering of Ministry of Education, College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, Jilin Province, PR China
E-mail: lzq@jlu.edu.cn
Tel: +86-431-85155201

c National Engineering Laboratory for AIDS Vaccine, College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, Jilin Province, PR China

d Department of Physics, Georgia Southern University, Statesboro, GA 30460, USA
E-mail: lma@georgiasouthern.edu

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.

Graphical abstract: Structure advantage and peroxidase activity enhancement of deuterohemin-peptide–inorganic hybrid flowers

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C6RA24192A
Article type
Paper
Submitted
29 Sep 2016
Accepted
26 Oct 2016
First published
27 Oct 2016

RSC Adv., 2016,6, 104265-104272

Permissions

Request permissions

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

Z. Zhao, J. Zhang, M. Wang, Z. Wang, L. Wang, L. Ma, X. Huang and Z. Li, RSC Adv., 2016, 6, 104265 DOI: 10.1039/C6RA24192A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements