Abstract
The importance of protein aggregation in providing environments for charge transport is now well established in natural systems that include the helix bundle that facilitates the light-induced proton pump in bacteriorhodopsin, as well as the membrane protein matrix that houses the reaction center of photosynthetic bacteria. In the present article, the authors describe a de novo 24-residue peptide having propensity for a high order of self-assembly. Moreover, the synthetic protein is capable of multistep electron-transfer involving an electrostatic docking agent. Other feature of the prevailing arrangement include an orientation for peptide chains that allows organization of N-terminal pyrene chromophores as dimers. Photooxidation of the self-assembled peptide bundle using methyl viologen (MV{sup 2+}) as electron acceptor is followed by charge migration to a remote site on the peptide provided by a tryptophan moiety.
Published Version
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