Probing Protein Adsorption on Model Surfaces

The ability to control nonspecific protein adsorption
at interfaces is a key issue in the design of
biosensors, assays, chromatographic separations and
implant materials. The research presented in this
manuscript focuses on the effect of surface
composition on the properties of adsorbed protein
layers and the probing of protein-protein
interactions both on adsorbed surfaces and in
solution. Monolayers of alkanethiols on gold formed
from solution self-assembly and microfluidic
patterning using poly(dimethyl) siloxane (PDMS)
served as platform for protein adsorption. We are
employed surface plasma resonance (SPR) imaging and
infrared reflection absorption spectroscopy (IRRAS)
to probe the conformation and orientation of adsorbed
proteins, as well as, the characterization of protein
layers.

Autorentext

Francis Nsiah
After graduating in Chemistry from University of Cape Coast,
Ghana, Dr. Nsiah went on to University of Alberta, Canada, where
he obtained his MSc and PhD by carrying out research into surface
characterization of thin films and protein-protein interactions.

Mark T. McDermott is Chemistry Professor at the University of
Alberta, Canada.

Klappentext

The ability to control nonspecific protein adsorption
at interfaces is a key issue in the design of
biosensors, assays, chromatographic separations and
implant materials. The research presented in this
manuscript focuses on the effect of surface
composition on the properties of adsorbed protein
layers and the probing of protein-protein
interactions both on adsorbed surfaces and in
solution. Monolayers of alkanethiols on gold formed
from solution self-assembly and microfluidic
patterning using poly(dimethyl) siloxane (PDMS)
served as platform for protein adsorption. We are
employed surface plasma resonance (SPR) imaging and
infrared reflection absorption spectroscopy (IRRAS)
to probe the conformation and orientation of adsorbed
proteins, as well as, the characterization of protein
layers.