Adsorption behaviour of amphiphilic polymers at hydrophobic surfaces: effects on protein adsorption.
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) (PEO) 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.
Freij-Larsson
C
C
Dept of Chemical Engineering II, Lund University, Chemical Center, Sweden.
Nylander
T
T
Jannasch
P
P
Wesslén
B
B
D000327:Adsorption; D001704:Biopolymers; D005340:Fibrinogen; D006801:Humans; D008689:Methacrylates; D018625:Microscopy, Atomic Force; D008961:Models, Structural; D015394:Molecular Structure; D008970:Molecular Weight; D011092:Polyethylene Glycols; D011095:Polyethylenes; D011108:Polymers; D011126:Polypropylenes; D011409:Propylene Glycols; D012709:Serum Albumin; D013052:Spectrometry, X-Ray Emission
D001704:Biopolymers; D008689:Methacrylates; C104019:Pluronic PE9400; D011095:Polyethylenes; D011108:Polymers; D011126:Polypropylenes; D011409:Propylene Glycols; D012709:Serum Albumin; C104020:poly(methylmethacrylate-co-ethylhexylmethacrylate); C012504:polypropylene glycol; D011092:Polyethylene Glycols; D005340:Fibrinogen