Self‐assembly of a series of dimetallic sequences constructed on a backbone with two successive tyrosine moieties ( Fmoc‐M 1 ‐M 2 ‐CO2H ) revealed that the resultant morphology is clearly dependent on the metal sequence, where Re‐containing sequences such as homometallic Fmoc‐Re‐Re‐CO2H specifically afforded amyloid‐like nanofibers. These findings further allowed to achieve the fibrillation of a longer metal sequence containing three different metals ( Fmoc‐Rh‐Pt‐Re‐Re‐CO2H ). Cyclic voltammetry of the fibrillated Fmoc‐Re‐Re‐CO2H demonstrated that the redox activity of the metal complexes in the sequence is preserved in the nanofibrous forms.