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Lectins at Interfaces-An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study.

Katrin Niegelhell1, Thomas Ganner2, Harald Plank3

  • 1Institute for Paper-, Pulp- and Fiber Technology, Graz University of Technology, Inffeldgasse 23, 8010 Graz, Austria. k.niegelhell@gmx.at.

Materials (Basel, Switzerland)
|November 25, 2018
PubMed
Summary

This study explores how plant lectins interact with various nanoscopic surfaces. Hydrophilic surfaces show resistance to protein adsorption, making them ideal for biosensors without blocking agents.

Keywords:
adsorptionbovine serum albumincellulose thin filmgoldlectinpolystyrenesurface plasmon resonance spectroscopy

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Area of Science:

  • Biochemistry
  • Materials Science
  • Surface Chemistry

Background:

  • Lectins are carbohydrate-binding proteins crucial for cell signaling and disease processes.
  • Lectins have applications in biosensors and glycan microarrays due to their specific glycan recognition.
  • Limited research exists on lectin interactions with diverse material surfaces.

Purpose of the Study:

  • To investigate the adsorption behavior of plant lectins (Concanavalin A, Ulex Europaeus Agglutinin-I) on various nanoscopic thin films.
  • To evaluate the influence of surface properties (hydrophobic, hydrophilic, charged) on lectin-surface interactions.
  • To identify suitable surfaces for biosensor applications by assessing protein adsorption resistance.

Main Methods:

  • Screening of lectin interactions with polystyrene, cellulose, N,N,N-trimethylchitosan chloride, and gold thin films.
  • Surface characterization using wettability, surface free energy, zeta potential, and morphology analysis.
  • Quantification of adsorbed protein using Atomic Force Microscopy (AFM) and Surface Plasmon Resonance (SPR) spectroscopy.

Main Results:

  • AFM imaging correlated well with protein adsorption mass.
  • Hydrophilic surfaces exhibited low protein adsorption and slow kinetics for all tested proteins, including controls like Bovine Serum Albumin.
  • These hydrophilic surfaces demonstrated resistance to non-specific protein interactions.

Conclusions:

  • Hydrophilic nanoscopic thin films are effective in preventing non-specific protein adsorption.
  • Such surfaces are promising candidates for biosensor development, potentially eliminating the need for blocking agents.
  • Understanding lectin-surface interactions is key for advancing biosensor technology and drug development.