Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Synthesis of Core@Brush microspheres by atom transfer radical polymerization for capturing phosphoprotein β-casein utilizing iron ion chelation and Schiff base bio-conjugation

Zeng, Hainan LU ; Hajizadeh, Solmaz LU orcid ; Yu, Xue ; Wan, Junfen ; Ye, Lei LU orcid and Cao, Xuejun (2022) In Separation and Purification Technology 295.
Abstract

This paper aims to design a highly efficient adsorbent to capture phosphoprotein in a facile way. One of the applications would be removing the allergenic β-casein from vaccines. To avoid the use of organic reagents and improve the capacity of immobilized metal ion affinity chromatography applied for bio-products at neutral pH, synergistic functional Core@Brush microspheres were designed utilizing iron ion chelation and Schiff base bio-conjugation. Surface-initiated atom transfer radical polymerization (ATRP) was used to grow polymer brushes, composed of one carbonyl-containing functional monomer diacetone acrylamide (DAAM) and the other monomer glycidyl methacrylate (GMA), on active microspheres as the cores. Then the material was... (More)

This paper aims to design a highly efficient adsorbent to capture phosphoprotein in a facile way. One of the applications would be removing the allergenic β-casein from vaccines. To avoid the use of organic reagents and improve the capacity of immobilized metal ion affinity chromatography applied for bio-products at neutral pH, synergistic functional Core@Brush microspheres were designed utilizing iron ion chelation and Schiff base bio-conjugation. Surface-initiated atom transfer radical polymerization (ATRP) was used to grow polymer brushes, composed of one carbonyl-containing functional monomer diacetone acrylamide (DAAM) and the other monomer glycidyl methacrylate (GMA), on active microspheres as the cores. Then the material was chemically modified with iminodiacetic acid and chelated with Fe(III). Adsorption studies show that the Core@Brush microspheres can selectively distinguish phosphoproteins with non-phosphoproteins, and has an excellent adsorption capacity over 2000 μg/mg towards β-casein owing to a large number of adsorption sites. The adsorption was well fitted to a pseudo-second-order kinetic model, indicating multi-valent chemisorption. The assumption is that β-casein was selectively captured by the synergistic function of stable iron ion chelation and reversible Schiff base bio-conjugation, and the particle-protein-particle aggregates formed.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
ATRP, Core-brush structure, Metal ion chelation, Schiff base bio-conjugation, β-casein
in
Separation and Purification Technology
volume
295
article number
121252
pages
9 pages
publisher
Elsevier
external identifiers
  • scopus:85131097429
ISSN
1383-5866
DOI
10.1016/j.seppur.2022.121252
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2022 Elsevier B.V.
id
afd8a1d5-ee88-436a-a375-c791544d159f
date added to LUP
2022-09-29 14:20:06
date last changed
2023-11-07 09:56:25
@article{afd8a1d5-ee88-436a-a375-c791544d159f,
  abstract     = {{<p>This paper aims to design a highly efficient adsorbent to capture phosphoprotein in a facile way. One of the applications would be removing the allergenic β-casein from vaccines. To avoid the use of organic reagents and improve the capacity of immobilized metal ion affinity chromatography applied for bio-products at neutral pH, synergistic functional Core@Brush microspheres were designed utilizing iron ion chelation and Schiff base bio-conjugation. Surface-initiated atom transfer radical polymerization (ATRP) was used to grow polymer brushes, composed of one carbonyl-containing functional monomer diacetone acrylamide (DAAM) and the other monomer glycidyl methacrylate (GMA), on active microspheres as the cores. Then the material was chemically modified with iminodiacetic acid and chelated with Fe(III). Adsorption studies show that the Core@Brush microspheres can selectively distinguish phosphoproteins with non-phosphoproteins, and has an excellent adsorption capacity over 2000 μg/mg towards β-casein owing to a large number of adsorption sites. The adsorption was well fitted to a pseudo-second-order kinetic model, indicating multi-valent chemisorption. The assumption is that β-casein was selectively captured by the synergistic function of stable iron ion chelation and reversible Schiff base bio-conjugation, and the particle-protein-particle aggregates formed.</p>}},
  author       = {{Zeng, Hainan and Hajizadeh, Solmaz and Yu, Xue and Wan, Junfen and Ye, Lei and Cao, Xuejun}},
  issn         = {{1383-5866}},
  keywords     = {{ATRP; Core-brush structure; Metal ion chelation; Schiff base bio-conjugation; β-casein}},
  language     = {{eng}},
  month        = {{08}},
  publisher    = {{Elsevier}},
  series       = {{Separation and Purification Technology}},
  title        = {{Synthesis of Core@Brush microspheres by atom transfer radical polymerization for capturing phosphoprotein β-casein utilizing iron ion chelation and Schiff base bio-conjugation}},
  url          = {{http://dx.doi.org/10.1016/j.seppur.2022.121252}},
  doi          = {{10.1016/j.seppur.2022.121252}},
  volume       = {{295}},
  year         = {{2022}},
}