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Adsorption behaviour of amphiphilic polymers at hydrophobic surfaces: Effects on protein adsorption

Freij-Larsson, Christina; Nylander, Tommy LU ; Jannasch, Patric LU and Wesslén, Bengt LU (1996) In Biomaterials 17(22). p.2199-2207
Abstract
The adsorption of four different amphiphilic polymers to a model surface has been studied, and the effects of the adsorbed amphiphiles on the subsequent adsorption of fibrinogen (Fg) and human serum albumin (HSA) at the surfaces were investigated. The amphiphilic polymers were one commercially available ABA block copolymer, Pluronic PE9400 (PE94), composed of poly(ethylene oxide) (A-blocks) and poly(propylene oxide) (B-block), and three graft copolymers, two with backbones of poly(styrene-co-acrylamide) (STY) and one with a backbone of poly(methyl methacrylate-co-ethylhexyl methacrylate) (ACRY). The backbones carried poly(ethylene oxide) (PEG) grafts, The model surface was a hydrophobic methylated silica surface (HMS).

The... (More)
The adsorption of four different amphiphilic polymers to a model surface has been studied, and the effects of the adsorbed amphiphiles on the subsequent adsorption of fibrinogen (Fg) and human serum albumin (HSA) at the surfaces were investigated. The amphiphilic polymers were one commercially available ABA block copolymer, Pluronic PE9400 (PE94), composed of poly(ethylene oxide) (A-blocks) and poly(propylene oxide) (B-block), and three graft copolymers, two with backbones of poly(styrene-co-acrylamide) (STY) and one with a backbone of poly(methyl methacrylate-co-ethylhexyl methacrylate) (ACRY). The backbones carried poly(ethylene oxide) (PEG) grafts, The model surface was a hydrophobic methylated silica surface (HMS).

The amphiphilic polymers were adsorbed at the HMS surface from an ethanol/water solution. The adsorption process was monitored by ellipsometry. After rinsing with phosphate buffered saline (PBS), protein was added and the continued adsorption measured by ellipsometry. Surfaces modified by adsorption of the amphiphilic polymers were also characterized by contact angle measurements and X-ray photoelectron spectroscopy (XPS). According to these measurements the amphiphilic polymers adsorbed in significant amounts at the HMS surface. A limited study by atomic force microscopy (AFM), as well as the XPS measurements, suggests that both single molecules and micellar aggregates adsorb at the surface. ACRY and PE94 gave the highest levels of adsorption. As compared to the Pluronic block copolymer the graft copolymers were more strongly attached to the HMS surface, as shown by less desorption on rinsing with solvent.



The ellipsometric results show that the adsorption of HSA and Fg at HMS surfaces containing preadsorbed amphiphilic polymer was significantly reduced as compared to the bare HMS surface. ACRY and PE94 showed the largest effects. Both polymers gave more than a 20-fold reduction of the Fg adsorption and a 10-fold reduction of the HSA adsorption. The STY polymers reduced the protein adsorption by a factor of 2-3. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomaterials
volume
17
issue
22
pages
2199 - 2207
publisher
Elsevier
external identifiers
  • scopus:0030298453
ISSN
1878-5905
DOI
10.1016/0142-9612(96)00050-6
language
English
LU publication?
yes
id
52d546a6-29ab-44d0-baea-6c5ec1b3348e (old id 149585)
date added to LUP
2007-07-13 11:43:14
date last changed
2017-07-30 03:32:06
@article{52d546a6-29ab-44d0-baea-6c5ec1b3348e,
  abstract     = {The adsorption of four different amphiphilic polymers to a model surface has been studied, and the effects of the adsorbed amphiphiles on the subsequent adsorption of fibrinogen (Fg) and human serum albumin (HSA) at the surfaces were investigated. The amphiphilic polymers were one commercially available ABA block copolymer, Pluronic PE9400 (PE94), composed of poly(ethylene oxide) (A-blocks) and poly(propylene oxide) (B-block), and three graft copolymers, two with backbones of poly(styrene-co-acrylamide) (STY) and one with a backbone of poly(methyl methacrylate-co-ethylhexyl methacrylate) (ACRY). The backbones carried poly(ethylene oxide) (PEG) grafts, The model surface was a hydrophobic methylated silica surface (HMS). <br/><br>
The amphiphilic polymers were adsorbed at the HMS surface from an ethanol/water solution. The adsorption process was monitored by ellipsometry. After rinsing with phosphate buffered saline (PBS), protein was added and the continued adsorption measured by ellipsometry. Surfaces modified by adsorption of the amphiphilic polymers were also characterized by contact angle measurements and X-ray photoelectron spectroscopy (XPS). According to these measurements the amphiphilic polymers adsorbed in significant amounts at the HMS surface. A limited study by atomic force microscopy (AFM), as well as the XPS measurements, suggests that both single molecules and micellar aggregates adsorb at the surface. ACRY and PE94 gave the highest levels of adsorption. As compared to the Pluronic block copolymer the graft copolymers were more strongly attached to the HMS surface, as shown by less desorption on rinsing with solvent.<br/><br>
<br/><br>
The ellipsometric results show that the adsorption of HSA and Fg at HMS surfaces containing preadsorbed amphiphilic polymer was significantly reduced as compared to the bare HMS surface. ACRY and PE94 showed the largest effects. Both polymers gave more than a 20-fold reduction of the Fg adsorption and a 10-fold reduction of the HSA adsorption. The STY polymers reduced the protein adsorption by a factor of 2-3.},
  author       = {Freij-Larsson, Christina and Nylander, Tommy and Jannasch, Patric and Wesslén, Bengt},
  issn         = {1878-5905},
  language     = {eng},
  number       = {22},
  pages        = {2199--2207},
  publisher    = {Elsevier},
  series       = {Biomaterials},
  title        = {Adsorption behaviour of amphiphilic polymers at hydrophobic surfaces: Effects on protein adsorption},
  url          = {http://dx.doi.org/10.1016/0142-9612(96)00050-6},
  volume       = {17},
  year         = {1996},
}