Polymer-protein giant amphiphiles by metal-to-ligand coordination

A new class of amphiphilic mols., viz., giant amphiphiles, which consist of an enzyme or a protein head group connected to a hydrophobic polymeric tail has been synthesized. This new generation of amphiphiles, behave like their super- and low mol. wt. analogs and also form catalytically active, well-defined assemblies in aq. soln. A new strategy was described for the synthesis of precisely defined, monodispersed enzyme-polymer hybrids using a more dynamic, highly controlled, supramol. approach, viz., the metal-to-ligand coordination. Both components (the protein and the polymers) have been functionalized with a terpyridine moiety and subsequently treated with various metal ions (e.g. Ru(III)Cl3, FeCl2) in order to create giant amphiphilic mols. and bis-terpyridine protein-metal complexes. The catalytic activity and the assembling properties of these amphiphiles as compared to those of their covalent analogs were discussed.