Unlike conventional self-assembled monolayers, reversible self-assembled monolayers(rSAMs) are formed through reversible ionic interactions. This allows switching betweenassembly and disassembly in response to pH changes and allows molecules to movelaterally within the layer. rSAMs are an attractive biomimetic platform due to thesedynamic properties. In this thesis, fluorescence measurements were used to evaluate ifrSAMs on glass could be used to detect SARS-CoV-2 proteins. The rSAMs werefunctionalized with sialic acid (SA) and the ACE2 epitope α2 (E2α2) to emulate viralrecognition at cell membranes. Surface behaviour was characterized using fluorescencespectroscopy and water contact angle measurements. Two fluorophores were used:fluorescein (FAM) was incorporated into the rSAM structure and Alexa Fluor 647(AF647) labelled RBD protein. The reversible fluorescence responses observed during pHcycling were an indication of assembly and disassembly processes. Signals recorded in theFAM region mainly captured shifts in surface organization, hydration and molecularrearrangements within the monolayer, while AF647 provided a more direct indication ofprotein retention after rinsing. Ligand composition and density influenced the observedresponses. In particular, surfaces containing 10% E2α2, frequently produced more stableand reproducible signals than those with higher ligand densities. Suggesting thatfluorescence responses are not determined solely by how much ligand is present but byhow accessible the molecules are and how they are arranged on the surface. CombiningSA and E2α2 improved the post-rinse signal, pointing to changes in protein-surfaceinteractions. Taken together, these findings highlight that fluorescence responses emergefrom multiple effects of ligand composition, density, spatial organization within the rSAMand hydration, illustrating the complex nature of multivalent protein–surface interactions.