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Abstract Polyproline II (PPII) peptide sequences are recognized as promising biomaterials because of their attractive antifouling properties. However, the mechanisms behind their antifouling behavior have not been fully characterized. In this work we show that PPII peptide coverage, controlled by adsorption time, significantly reduces the fouling of bovine serum albumin (BSA, a model foulant). In addition, guest residues introduced into the PPII sequence are shown to significantly impact BSA adsorption as well as human mesenchymal stem cell (hMSC) spreading. This research will help guide future PPII peptide designs for incorporation into novel biomaterials. Graphical abstract 

Abstract The significance of easily detecting rare earth elements (REEs) has increased due to the growing demand for REEs. Addressing this need, we present an innovative electrochemical biosensor, focusing on cerium as a model REE. This biosensor utilizes a modified EF‐hand loop peptide sequence, incorporating cysteine for covalent attachment to a gold working electrode and tyrosine as an electrochemically active amino acid. The sensor was designed such that binding to cerium induces a conformational change in the peptide, affecting tyrosine's proximity to the electrode surface, modulating the current. A calibration curve was generated from cyclic voltammetry current peaks at ~0.55–0.65 V versus a silver pseudo‐reference electrode, with cerium concentrations ranging from 0 to 67 μM in artificial urine. The sensor exhibited a biologically relevant limit of detection of 35 μM and a sensitivity of −0.0024 ± 0.002 (μA μM)⁻¹. These findings offer insights into designing peptide sequences for electrochemical biosensing.