Viscoelastic modeling of highly hydrated laminin layers at homogeneous and nanostructured surfaces: quantification of protein layer properties using QCM-D and SPR.
Journal article, 2007

The adsorption of proteins at material surfaces is important in applications such as biomaterials, drug delivery, and diagnostics. The interaction of cells with artificial surfaces is mediated through adsorbed proteins, where the type of protein, amount, orientation, and conformation are of consequence for the cell response. Laminin, an important cell adhesive protein that is central in developmental biology, is studied by a combination of quartz crystal microbalance with dissipation (QCM-D) and surface plasmon resonance (SPR) to characterize the adsorption of laminin on surfaces of different surface chemistries. The combination of these two techniques allows for the determination of the thickness and effective density of the protein layer as well as the adsorbed mass and viscoelastic properties. We also evaluate the capacity of QCM-D to be used as a quantitative technique on a nanostructured surface, where protein is adsorbed specifically in a nanopattern exploiting PLL-g-PEG as a protein-resistant background. We show that laminin forms a highly hydrated protein layer with different characteristics depending on the underlying substrate. Using a combination of QCM-D and atomic force microscopy (AFM) data from nanostructured surfaces, we model laminin and antibody binding to nanometer-scale patches. A higher amount of laminin was found to adsorb in a thicker layer of a lower effective density in nanopatches compared to equivalent homogeneous surfaces. These results suggest that modeling of QCM-D data of soft viscoelastic layers arranged in nanopatterns may be applied where an independent measure of the "dry" mass is known.

chemistry

chemistry

Surface Properties

Silicon Dioxide

Nanostructures

chemistry

Gold

Elasticity

Laminin

chemistry

Biological

chemistry

Water

Models

Surface Plasmon Resonance

Viscosity

Quartz

Author

Jenny Malmström

Hossein Agheli

Peter Kingshott

Duncan S Sutherland

Langmuir

07437463 (ISSN) 15205827 (eISSN)

Vol. 23 19 9760-8

Subject Categories

Biological Sciences

DOI

10.1021/la701233y

PubMed

17691829

More information

Created

10/10/2017