Molecular recognition of cytochrome c by designed receptors for generation of in vivo and in vitro functions

Cytochrome c is a common guest in biological protein recognition processes and works not as an enzyme, but as an electron carrier in biological respiration. Although this is a relatively small protein, its structure is too complicated to be easily recognized by common synthetic receptors. This review is an overview of the molecular recognition of cytochrome c by synthetic receptors and highlights two examples exhibiting in vivo and in vitro non-biological functions: (i) crown ether receptors effectively interact with cationic residues via multiple crown ether complexations and (ii) dendrimer receptors strongly bind with a negatively charged patch via complementary electrostatic interactions. These designed receptors offer effective cytochrome c recognition to generate non-biological catalytic activity and in cell functions.