Protein Surface Mimetics: Understanding How Ruthenium Tris(Bipyridines) Interact with Proteins.
Protein Surface Mimetics: Understanding How Ruthenium Tris(Bipyridines) Interact with Proteins.
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DOI：
10.1002/cbic.201600552
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发表时间：
2017-01-17
期刊：
影响因子：
--
通讯作者：
Wilson AJ
中科院分区：
文献类型：
--
作者：
Hewitt SH;Filby MH;Hayes E;Kuhn LT;Kalverda AP;Webb ME;Wilson AJ
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 natural abundance 1H,15N HSQC NMR experiments are consistent with surface mimetics binding to cyt c in similar manner to CCP. This provides a framework for understanding recognition of proteins by supramolecular receptors and informing the design of ligands superior to the protein partners upon which they are inspired.
影响因子：
3.2
作者：
Margulies, David;Opatowsky, Yarden;Fletcher, Steven;Saraogi, Ishu;Tsou, Lun K.;Saha, Sourav;Lax, Irit;Schlessinger, Joseph;Hamilton, Andrew D.
通讯作者：
Hamilton, Andrew D.