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We have used albumin-modified atomic force microscope (AFM) tips to probe interactions with a range of hydrophilic polymer brush surfaces and protein. Copolymers of poly(ethylene oxide)−poly(propylene oxide)−poly(ethylene oxide) (PEO−PPO−PEO) (Pluronics) adsorbed onto polymer interfaces have been shown in previous studies to modify adsorption properties of blood components [using surface plasmon resonance (SPR) and AFM]. Here we have employed protein-coated AFM probes to study a series of PEO−PPO−PEO-coated interfaces prepared with a range of PEO and PPO molecular weights. Subsequent force−distance experiments have shown a good correlation between the forces of adhesion of an albumin-functionalized AFM probe with the various PEO−PPO−PEO surfaces and the adsorption trends of albumin onto these polymeric surfaces observed with SPR. The data suggest that the size of the hydrophobic PPO segment of the Pluronic is a major determinant of the polymer protein resistance properties. In addition, as the PEO layer density increased, a reduction of interaction force was measured because of the formation of a steric barrier from the PEO polymer brush. Such studies suggest that AFM may be employed as a novel method to assess “biocompatibility” and to rapidly screen surface-engineered surfaces with micrometer spatial resolution.