The self-assembly of tyrosyl bolaamphiphiles is exploited to create a colloidal protein-like host matrix, upon which sacrificial electron-donor molecules associate to create a photosystem II (PSII) mimetic electron-relay system. This system harnesses the tyrosine phenol groups abundant on the surface of the assemblies to mediate photoinduced intermolecular electron transfer. Compared with the l-tyrosine molecules, the tyrosyl bolaamphiphile assembly facilitates electron transfer from the sacrificial electron donor to the oxidized photosensitizer. The enhanced electron relay is likely to be driven by the host function of the assembly associated with the sacrificial electron donor and by the suppression of the oxidative cross-linking of phenoxyl radicals. The tyrosyl bolaamphiphile assembly is advantageous in the construction of a PSII mimetic system with a protein-like nature and displaying biochemical functions.
Keywords: bolaamphiphiles; electron transfer; photochemistry; protein models; self-assembly.
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