Advanced

Synthesis and characterization of epitope-imprinted polymers for purification of human hemoglobin.

Bagan Navarro, Hector LU ; Zhou, Tongchang LU ; Eriksson, Nélida Leiva LU ; Bülow, Leif LU and Ye, Lei LU (2017) In RSC Advances 7(66). p.41705-41712
Abstract
One promising method to prepare protein-selective polymers is the epitope-imprinting approach, where surface-accessible peptides from a target protein are used as templates to create surface-exposed binding sites on molecularly imprinted polymers (MIPs). However, selection of a suitable peptide target is not always straightforward, and synthesis of peptide on a large scale can be costly. In this work, we developed a new approach that can be used to select peptide epitopes on protein surface to be used as templates to prepare protein-selective MIPs. In this case study, human hemoglobin (Hb) was immobilized on silica nanoparticles and then fragmented by tryptic digestion. The particle-supported peptides were then used as templates to... (More)
One promising method to prepare protein-selective polymers is the epitope-imprinting approach, where surface-accessible peptides from a target protein are used as templates to create surface-exposed binding sites on molecularly imprinted polymers (MIPs). However, selection of a suitable peptide target is not always straightforward, and synthesis of peptide on a large scale can be costly. In this work, we developed a new approach that can be used to select peptide epitopes on protein surface to be used as templates to prepare protein-selective MIPs. In this case study, human hemoglobin (Hb) was immobilized on silica nanoparticles and then fragmented by tryptic digestion. The particle-supported peptides were then used as templates to synthesize the Hb-selective MIPs, which were obtained after removal of the silica support and the peptides. The MIPs were tested in equilibrium binding experiments to evaluate their protein separation performance. The new surface imprinted MIPs displayed high selectivity for Hb, and was able to separate different variants of Hb from protein mixtures and crude cell extracts. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
RSC Advances
volume
7
issue
66
pages
41705 - 41712
publisher
Royal Society of Chemistry
external identifiers
  • scopus:85028751283
  • wos:000409147000045
ISSN
2046-2069
DOI
10.1039/C7RA07674F
language
English
LU publication?
yes
id
16b8a7a7-fbc8-47c1-8dec-4b9a31fc46fc
date added to LUP
2017-09-14 10:54:19
date last changed
2018-01-16 13:25:40
@article{16b8a7a7-fbc8-47c1-8dec-4b9a31fc46fc,
  abstract     = {One promising method to prepare protein-selective polymers is the epitope-imprinting approach, where surface-accessible peptides from a target protein are used as templates to create surface-exposed binding sites on molecularly imprinted polymers (MIPs). However, selection of a suitable peptide target is not always straightforward, and synthesis of peptide on a large scale can be costly. In this work, we developed a new approach that can be used to select peptide epitopes on protein surface to be used as templates to prepare protein-selective MIPs. In this case study, human hemoglobin (Hb) was immobilized on silica nanoparticles and then fragmented by tryptic digestion. The particle-supported peptides were then used as templates to synthesize the Hb-selective MIPs, which were obtained after removal of the silica support and the peptides. The MIPs were tested in equilibrium binding experiments to evaluate their protein separation performance. The new surface imprinted MIPs displayed high selectivity for Hb, and was able to separate different variants of Hb from protein mixtures and crude cell extracts.},
  author       = {Bagan Navarro, Hector and Zhou, Tongchang and Eriksson, Nélida Leiva and Bülow, Leif and Ye, Lei},
  issn         = {2046-2069},
  language     = {eng},
  number       = {66},
  pages        = {41705--41712},
  publisher    = {Royal Society of Chemistry},
  series       = {RSC Advances},
  title        = {Synthesis and characterization of epitope-imprinted polymers for purification of human hemoglobin.},
  url          = {http://dx.doi.org/10.1039/C7RA07674F},
  volume       = {7},
  year         = {2017},
}