A Novel N‐Substituted Pyrrole Based Surface Modification for Biosensing. Issue 15 (18th May 2018)

• Record Type: Journal Article
• Authors: Rüger, Fabian; Schäfer, Jens; Bakowski, Udo; Keusgen, Michael; Vornicescu, Doru
• Other Names: Wagner Patrick guestEditor.; Keusgen Michael guestEditor.; Doll Theodor guestEditor.; Wagner Torsten guestEditor.; Schöning Michael J. guestEditor.
• Is Part Of: Physica status solidi. Volume 215:Issue 15(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-05-18
• Subjects: atomic force microscopy (AFM) -- electro polymerization -- N‐substituted pyrroles -- poly‐pyrroles (PPy) -- surface plasmon resonance (SPR); Solid state physics -- Periodicals; Solids -- Industrial applications -- Periodicals; 530.41
• DOI: 10.1002/pssa.201800030
• Languages: English
• ISSNs: 1862-6300

Abstract

Abstract : Immobilization of proteins, mostly antigens, antibodies or enzymes on a solid surface, is one of the most important steps in the development of every biosensor. Different chemical methods as well as site‐directed strategies have been developed in order to obtain highest functionality and stability for the sensoric device. In the present work, a novel method for the immobilization of biomolecules on a surface plasmon resonance (SPR) device is described. New N ‐substituted pyrroles are synthesized and deposited on a gold surface using electrochemical polymerization. To evaluate the established four different surfaces, the binding behavior between a fusion protein consisting of the lectin concanavalin A (ConA) as well as streptavidin (Sav) binding domains and the sugar mannan, which has been chemically coupled to the poly‐pyrrole (PPy) surface is investigated. A pyrrole‐ N ‐C16 /pyrrole co‐polymer surface as well as a pyrrol‐1‐yl hexanoic acid/pyrrole (PHCP) surface give best results. Abstract : Different N ‐substituted pyrroles are synthesized and via electro‐polymerization deposited on a surface plasmon resonance (SPR) biosensor. Their use to create a novel binding surface for development of assays like sugar‐lectin binding assays is studied by SPR technology. The pyrrole‐N‐C16 co‐polymer surface as well as the pyrrole/6‐(1H‐pyrrol‐1‐yl) hexanoic acid co‐polymer (PHCP) with and without chemical activation are suitable for binding assays.