Next Article in Journal
Determining k-Value with Regard to Freeze-Thaw Resistance of Concretes Containing GGBS
Next Article in Special Issue
Green Procedure to Manufacture Nanoparticle-Decorated Paper Substrates
Previous Article in Journal
Theoretical Study of Hydrogen on LaFeO3 (010) Surface Adsorption and Subsurface Diffusion
Previous Article in Special Issue
Physical and Morphological Changes of Poly(tetrafluoroethylene) after Using Non-Thermal Plasma-Treatments
Article Menu

Export Article

Open AccessArticle
Materials 2018, 11(12), 2348; https://doi.org/10.3390/ma11122348

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

1
Institute for Paper-, Pulp- and Fiber Technology, Graz University of Technology, Inffeldgasse 23, 8010 Graz, Austria
2
Institute for Electron Microscopy and Nanoanalysis, Graz University of Technology, Steyrergasse 17, 8010 Graz, Austria
3
Department of Obstetrics and Gynecology, Medical University of Graz, Auenbruggerplatz 14, 8036 Graz, Austria
*
Author to whom correspondence should be addressed.
Received: 27 September 2018 / Revised: 8 November 2018 / Accepted: 17 November 2018 / Published: 22 November 2018
(This article belongs to the Special Issue Surface Modification to Improve Properties of Materials)
Full-Text   |   PDF [6765 KB, uploaded 22 November 2018]   |  

Abstract

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. View Full-Text
Keywords: lectin; bovine serum albumin; adsorption; cellulose thin film; polystyrene; gold; surface plasmon resonance spectroscopy lectin; bovine serum albumin; adsorption; cellulose thin film; polystyrene; gold; surface plasmon resonance spectroscopy
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Niegelhell, K.; Ganner, T.; Plank, H.; Jantscher-Krenn, E.; Spirk, S. Lectins at Interfaces—An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study. Materials 2018, 11, 2348.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Materials EISSN 1996-1944 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top