Protein adsorption at nanopatterned surfaces studied by quartz crystal microbalance with dissipation and surface plasmon resonance

J Phys Chem B. 2013 Sep 12;117(36):10376-83. doi: 10.1021/jp4038528. Epub 2013 Aug 28.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Cadherins / chemistry
  • Cadherins / metabolism
  • Nanostructures / chemistry*
  • Polyethylene Glycols / chemistry
  • Polylysine / analogs & derivatives
  • Polylysine / chemistry
  • Proteins / chemistry*
  • Proteins / metabolism
  • Quartz Crystal Microbalance Techniques
  • Surface Plasmon Resonance
  • Surface Properties
  • Vitronectin / chemistry
  • Vitronectin / metabolism

Substances

  • Cadherins
  • Proteins
  • Vitronectin
  • polylysine-graft-(poly(ethylene glycol))
  • Polylysine
  • Polyethylene Glycols