Surface plasmon resonance for real time in situ analysis of protein adsorption to polymer surfaces.
The adsorption of a range of plasma proteins to metal and polymer surfaces has been examined using surface plasmon resonance (SPR). The adsorption of proteins was initially studied on the SPR silver sensor surface, and then on a model polystyrene film spun coated directly onto this substrate. In both cases, reproducible adsorption profiles for albumin were attained which compared well with corresponding atomic force microscopy (AFM) and ellipsometry data on protein monolayer packing and thickness respectively. The SPR data revealed the influence of concentration on both protein adsorption kinetics and the time for formation of a monolayer coating. SPR data also highlighted different adsorption kinetics and final monolayer SPR angle shift values for three plasma proteins which have been interpreted in terms of their molecular dimensions and orientation at the polymer interface. AFM data confirmed the presence of a closely packed protein layer for all three protein systems. These studies are discussed in terms of employing SPR in the study of protein interactions at surfaces which are important in the design and evaluation of novel biomedical polymeric materials.
Green
R J
RJ
Department of Pharmaceutical Sciences, University of Nottingham, University Park, UK.
Davies
J
J
Davies
M C
MC
Roberts
C J
CJ
Tendler
S J
SJ
D000327:Adsorption; D000418:Albumins / Q000737:chemistry; D001672:Biocompatible Materials / Q000737:chemistry*; D015374:Biosensing Techniques; D005340:Fibrinogen / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry; D011137:Polystyrenes / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012834:Silver / Q000737:chemistry; D013499:Surface Properties
D000418:Albumins; D001672:Biocompatible Materials; D007074:Immunoglobulin G; D011137:Polystyrenes; D011506:Proteins; D012834:Silver; D005340:Fibrinogen