Journal
CHEMICAL SCIENCE
Volume 2, Issue 12, Pages 2301-2305Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1sc00162k
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Funding
- Japan Society for Promotion of Science
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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.
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