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

Publication year: 2018
Authors: Niegelhell K. 1, Ganner T. 2, Plank H. 3, Jantscher-Krenn E. 4, Spirk S. 5
Affiliations:

1 - Institute for Paper-, Pulp- and Fiber Technology, Graz University of Technology, Inffeldgasse 23, 8010 Graz, Austria. k.niegelhell@gmx.at
2 - Institute for Electron Microscopy and Nanoanalysis, Graz University of Technology, Steyrergasse 17, 8010 Graz, Austria. Thomas.ganner@a1.net
3 - Institute for Electron Microscopy and Nanoanalysis, Graz University of Technology, Steyrergasse 17, 8010 Graz, Austria. harald.plank@felmi-zfe.at
4 - Department of Obstetrics and Gynecology, Medical University of Graz, Auenbruggerplatz 14, 8036 Graz, Austria. evelyn.jantscher-krenn@medunigraz.at
5 - Institute for Paper-, Pulp- and Fiber Technology, Graz University of Technology, Inffeldgasse 23, 8010 Graz, Austria. stefan.spirk@tugraz.at

Published in: Materials 2018, Vol. 11(12), p. 2348
doi: 10.3390/ma11122348

Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins employ their ability to recognize specific glycan epitopes in biosensors and glycan microarrays. While a lot of research has focused on lectin interaction with specific carbohydrates, the interaction potential of lectins with different types of surfaces has not been addressed extensively. Here, we screen the interaction of two specific plant lectins, Concanavalin A and Ulex Europaeus Agglutinin-I with different nanoscopic thin films. As a control, the same experiments were performed with Bovine Serum Albumin, a widely used marker for non-specific protein adsorption. In order to test the preferred type of interaction during adsorption, hydrophobic, hydrophilic and charged polymer films were explored, such as polystyrene, cellulose, N,-N,-N-trimethylchitosan chloride and gold, and characterized in terms of wettability, surface free energy, zeta potential and morphology. Atomic force microscopy images of surfaces after protein adsorption correlated very well with the observed mass of adsorbed protein. Surface plasmon resonance spectroscopy studies revealed low adsorbed amounts and slow kinetics for all of the investigated proteins for hydrophilic surfaces, making those resistant to non-specific interactions. As a consequence, they may serve as favorable supports for biosensors, since the use of blocking agents is not necessary.


MP-SPR keywords: anti-fouling properties, BSA adsorption, cellulose, hydrophobic interactions, protein-surface interaction, surface binding of lectins, surface coverage