The Structure of Benzenesulfonamide-Terminated Thiol on Gold Surfaces and the Interaction with Carbonic Anhydrase
(English)Manuscript (preprint) (Other academic)
A well-structured and robust biomolecular monolayer based upon a benzenesulfonamideterminated alkane thiol, to be used as a model system for molecular recognition processes, was prepared. The benzenesulfonamide-terminated thiol adsorbed onto gold substrates was characterized using X-ray photoelectron spectroscopy, near edge X-ray absorption fine structure spectroscopy, infrared-reflection absorption spectroscopy and ellipsometry. The results showed that the benzenesulfonamide-terminated alkane thiol forms a wellorganized molecular layer on the gold substrates. The orientation of the aromatic ring relative to the gold surface was investigated by means of the angle defined as the normal to the aromatic ring relative to the normal to the gold surface. It was shown that the average tilt angle is approximately 62º. In a second step, the benzenesulfonamideterminated thiol monolayer was exposed to carbonic anhydrase, which is an enzyme and a therapeutic target. Benzenesulfonamides are used in biomedical applications as inhibitors for carbonic anhydrase. Our purpose in this study was to investigate the recognition capability of the benzenesulfonamide when designed as a thiol monolayer. The interaction between the benzenesulfonamide-terminated monolayer and carbonic anhydrase was studied using ellipsometry and surface plasmon resonance. The results show that the benzenesulfonamide-terminated thiol adsorbed onto the gold substrates is able to bind carbonic anhydrase. The results also indicate that the interaction is specific.
IdentifiersURN: urn:nbn:se:liu:diva-71456OAI: oai:DiVA.org:liu-71456DiVA: diva2:449088