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.
Subject(s)
Amyloid/chemistry , Metal-Organic Frameworks/chemistry , Metals/chemistry , Nanofibers/chemistry , Microscopy, Electron, Scanning , Microscopy, Electron, Transmission , Oxidation-Reduction , Scattering, Radiation , Spectrum Analysis/methodsABSTRACT
A modular synthetic approach is reported for the synthesis of heterometallic metal-organic complex arrays (MOCAs). Modules of four metal centers containing three different metals copper(II), nickel(II), platinum(II), or ruthenium(II) are prepared using a solid-phase polypeptide synthesis technique and then linked in solution to make MOCAs of eight metal centers as linear, T-branched, and H-branched compounds. The MOCA molecular topologies thus have specific unique linear and branched sequences of metals along the peptide backbone.
