Isatin-induced increase in the affinity of human ferrochelatase and adrenodoxin reductase interaction.

ABSTRACT: Isatin (indol-2,3-dione) is an endogenous non-peptide regulator exhibiting a wide range of biological and pharmacological activities, which are poorly characterized in terms of their molecular mechanisms. Identification of many isatin-binding proteins in the mammalian brain and liver suggests that isatin may influence their functions. We have hypothesized that besides direct action on particular protein targets, isatin can act as a regulator of protein-protein interactions (PPIs). In this surface plasmon resonance-based biosensor study we have found that physiologically relevant concentrations of isatin (25-100 μM) increase affinity of interactions between human recombinant ferrochelatase (FECH) and NADPH-dependent adrenodoxin reductase (ADR). In the presence of increasing concentrations o

SUBMITTER: Ershov P 

PROVIDER: S-EPMC5699483 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature