Protein-resistant polyethylene-block-poly(ethylene glycol) (PE-b-PEG) copolymers of different molecular weights at various concentrations were compounded by melt blending with polypropylene (PP) polymers in order to enhance their antifouling properties. Phase separation of the PE-b-PEG copolymer and its migration to the surface of the PP blend, was confirmed by attenuated total reflectance-Fourier transform infrared, X-ray photoelectron spectroscopy, and static water contact angle measurements. Enrichment of PEG chains at the surface of the blends increased with increasing PE-b-PEG copolymer concentration and molecular weight. The PP blends compounded with PE-b-PEG copolymer having the lowest molecular weight (875 g mol 21 ), at the lowest concentration (1 wt %), gave the lowest bovine serum protein adsorption (30% less) compared to that of neat PP. At higher concentrations (5 and 10 wt %), and higher molecular weights (920, 1400, and 2250 g mol 21 ), the PE-b-PEG copolymers leached-out resulting in protein adsorption comparable to that of neat PP.Polypropylene (PP) is a widely used material for biomedical applications due to its many desirable properties, including low cost, ease of processing, and sterilization. 13 It finds extensive use in the biomedical field 14 as filtration membranes, 15 textiles/fabrics, and medical implants such as surgical meshes 16,17 and vascular prostheses. 18 These applications necessitate extraordinary wettability and protein repellency. 19 Wettability results from hydrophilic functional groups binding or interacting via H-bonding to water (H 2 O) molecules, leading to the formation of a highly hydrated layer of H 2 O molecules surrounding the hydrophilic groups. This hydrated layer results in steric hindrance to any incoming protein molecules, preventing their adsorption. 20Additional Supporting Information may be found in the online version of this article.