Poly(ethylene glycol) (PEG) is widely used to modulate the hydration states of biomaterials and is often applied to produce non-fouling surfaces. Here, we present X-ray scattering data which show that it is the surface segregation of PEG, not just its presence in the bulk, that makes this happen by influencing the hydrophilicity of PEG-containing substrates. We demonstrate a temperaturedependent trigger that transforms a PEG-containing substrate from a protein-adsorbing to a protein-repelling state. On films of poly(desaminotyrosyl-tyrosineco-PEG carbonate) with high (20 wt %) PEG content, in which very little protein adsorption would have been expected, quartz crystal microbalance (QCM) data showed significant adsorption of fibrinogen (Fg) and bovine serum albumin (BSA) at 8 °C. The surface became protein-repellent at 37.5 °C. When the same polymer was iodinated, the polymer was protein adsorbent, even when 37 wt % PEG was incorporated into the polymer backbone. This demonstrates that high PEG content by itself is not sufficient to repel proteins. By inhibiting phase separation either with iodine or by lowering the temperature, we show that PEG must phase separate and bloom to the surface in order to create an antifouling surface. These results suggest an opportunity to design materials with high-PEG content that can be switched from a protein-attractant to a protein-repellent state by inducing phase separation through a brief exposure to temperatures above their glass transition temperature.