Protein Surface Mimetics: Understanding How Ruthenium Tris(Bipyridines) Interact with Proteins.

ABSTRACT: Protein surface mimetics achieve high-affinity binding by exploiting a scaffold to project binding groups over a large area of solvent-exposed protein surface to make multiple cooperative noncovalent interactions. Such recognition is a prerequisite for competitive/orthosteric inhibition of protein-protein interactions (PPIs). This paper describes biophysical and structural studies on ruthenium(II) tris(bipyridine) surface mimetics that recognize cytochrome (cyt) c and inhibit the cyt c/cyt c peroxidase (CCP) PPI. Binding is electrostatically driven, with enhanced affinity achieved through enthalpic contributions thought to arise from the ability of the surface mimetics to make a greater number of noncovalent interactions than CCP with surface-exposed basic residues on cyt c. High-field nat

SUBMITTER: Hewitt SH 

PROVIDER: S-EPMC5347857 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature