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Updated: May 9, 2026
Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Protein adsorption at nanopatterned surfaces studied by quartz crystal microbalance with dissipation and surface
Stine H Kristensen1, Gitte A Pedersen, Lene N Nejsum
1Interdisciplinary Nanoscience Center (iNANO) and ‡Department of Molecular Biology and Genetics, Aarhus University , Denmark.
Abstract:
This paper presents the use of the quartz crystal microbalance with dissipation (QCM-D) combined with surface plasmon resonance (SPR) to probe protein adsorption at nanopatterned surfaces. Three different types of adsorbing materials, representing rigid discrete nanoparticles, dense protein films, and soft low density films have been studied on systematic varied circular nanostructures in the 100-1000 nm size range. Analysis and quantification of the QCM-D response from larger nanostructures could be understood and quantified in the same way as for homogeneous surfaces, while that for nanostructures of 100 and 200 nm diameter was significantly underestimated. Our findings suggest a size limitation of those techniques in analysis of adsorption at nanofeatures.
