Amyloid-like Nanofibrillation of Metal-Organic Complex Arrays Ruled by Their Precisely Designed Metal Sequences

Abstract

Self-assembly of a series of dimetallic sequences constructed on a backbone with two successive tyrosine moieties (Fmoc-M¹ -M² -CO₂ H) revealed that the resultant morphology is clearly dependent on the metal sequence, where Re-containing sequences such as homometallic Fmoc-Re-Re-CO₂ H 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-CO₂ H). Cyclic voltammetry of the fibrillated Fmoc-Re-Re-CO₂ H demonstrated that the redox activity of the metal complexes in the sequence is preserved in the nanofibrous forms.

Keywords: amyloid-like nano-fibrillation; metal sequence; peptides; redox reaction; ß-sheet.