It binds to antithrombin III (ATIII), which then in turn can inactivate thrombin (Factor IIa) and Factor Xa, two key coagulation proteins involved in the blood clotting process. Heparin is also known to possess anti-inflammatory effects, such as its interactions with the complement pathway, its ability to reduce neutrophil adhesion to the endothelium, and its possible interaction with NF-κB. However, the potent anti-coagulant effect of heparin prevents its use as a therapeutic agent for anti-inflammatory purposes due to the danger of increased bleeding as a side effect. In this study, we investigated the potential use of sulfated or carboxylated polyglycerols (dendritic and linear versions) as heparin analogues and analyzed their binding to proinflammatory proteins such as TSLP and FN via surface plasmon resonance spectroscopy (SPR). In this preliminary analysis we sought a better understanding of how binding would be influenced by charged groups, the difference between carboxyl and sulfate groups, and polymer architecture. We then aimed to build on the SPR results to assess the investigated polyglycerols' potential as antiinflammatory agents in type 2 inflammation.