EGFR and glioblastoma: The lack of disulfide bonds and internal cysteines, rapid folding properties and high stability of affibody molecules facilitate their conjugation with different radionuclides or fluorophores.20 Moreover, the high binding affinity (pM to nM range) of these molecules to wild‐type EGFR, as well as EGFRvIII, their small size (resulting in rapid clearance from the circulation with predominantly renal excretion in vivo), and good tumor penetration make them ideal targeting agents for GBM therapy.21