A method of poly(ethylene glycol) (PEG) conjugation is known as PEGylation, which has been employed to deliver therapeutic drugs, proteins, or nanoparticles by considering the intrinsic non- or very low immunogenic property of PEG. However, PEG has its weaknesses, and one major concern is the potential immunogenicity of PEGylated proteins. Because of its hydrophilicity, poly(sarcosine) (P(Sar)) may be an attractive-and superior-substitute for PEG. In the present study, we designed a double hydrophilic diblock copolymer, methoxy-PEG--P(Sar) ( = 5-55) (mPEG-P(Sar) ), and synthesized a triblock copolymer with hydrophobic poly(l-isoleucine) (P(Ile)). We validated that double hydrophilic mPEG-P(Sar) block copolymers suppressed the specific binding of three monoclonal anti-PEG antibodies (anti-PEG mAbs) to PEG. The results of our indirect ELISAs indicate that P(Sar) significantly helps to reduce the binding of anti-PEG mAbs to PEG. Importantly, the steady suppression of this binding was made possible, in part, thanks to the maximum number of sarcosine units in the triblock copolymer, as evidenced by sandwich ELISA and biolayer interferometry assay (BLI): the intrinsic hydrophilicity of P(Sar) had a clear supportive effect on PEG. Finally, because we used P(Ile) as a hydrophobic block, PEG-P(Sar) might be an attractive alternative to PEG in the search for protein shields that minimize the immunogenicity of PEGylated proteins.