| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1371712 | Bioorganic & Medicinal Chemistry Letters | 2012 | 5 Pages |
Abstract
We examined the relationship between the structures of hetero-/homoleptic ruthenium(II) tris(bipyridine) metal complexes (RuII(bpy)3) and their binding properties for α-chymotrypsin (ChT) and cytochrome c (cyt c). Heteroleptic compound 1a binds to both ChT and cyt c in 1:1 ratio, whereas homoleptic 2 forms 1:2 protein complex with ChT but 1:1 complex with cyt c. These results suggest that the structure of the recognition cavity in RuII(bpy)3 can be designed for shape complementarity to the targeted proteins. In addition, RuII(bpy)3 complexes were found to be potent inhibitors of cyt c reduction and to permeate A549 cells.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Yoshinobu Yamaguchi, Nobuo Kato, Hideki Azuma, Takeshi Nagasaki, Junko Ohkanda,