This dissertation focuses on the development and application of polyglycerol (PG)-based polymers for the modulation of type 2 inflammation as well as their use as innovative materials for biosensor analysis using surface plasmon resonance (SPR) spectroscopy. Dysregulated type 2 inflammation forms the pathophysiological basis of atopic diseases such as atopic dermatitis or allergic asthma. Among other factors, disease progression is influenced by increased levels of cytokines such as thymic stromal lymphopoietin (TSLP) and extracellular matrix proteins such as fibronectin (FN). Both molecules exhibit cationic regions on their surface and therefore offer potential for electrostatic interactions with polyanions. In the first part of this work, linear and dendritic PGs were carboxylated and sulfated and subsequently analyzed via SPR with regard to their interactions with FN and TSLP. Highly sulfated polymers showed high-affinity binding to both target molecules. The most promising polymer candidates were further investigated to assess the extent to which they can modulate or suppress the inflammatory effects mediated by TSLP and FN. Even at low concentrations (10 ng/mL), TSLP-neutralizing effects were observed with respect to the proinflammatory type 2 polarization of T cells. In contrast, significantly higher concentrations were required for FN-neutralizing effects in inflamed bronchial epithelium tissue models. As these biochemical investigations require highly sensitive and selective analytical methods, the second part of the work focused on the development of innovative SPR biosensors based on a PG-polyethylene glycol (PEG) hydrogel. The main requirements were high ligand loading capacity and minimal nonspecific binding. Heparin-binding proteins such as the described FN or lectins often lead to nonspecific interactions with the carboxymethyldextran (CMD) matrix of conventional SPR biosensors, which complicates analysis. In contrast, the newly developed PG-PEG SPR biosensors exhibited significantly reduced nonspecific binding while maintaining high loading capacity. Furthermore, they were validated for the analysis of both small (222 Da) and large (150 kDa) biomolecules by comparing the determined binding constants with those obtained using CMD-based biosensors.
