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Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2'-bipyridine and its 5,5'-dicarboxylic acid derivatives
Abstract
Members of a series of 2,2'-bipyridines have been synthesized and tested as inhibitors of prolyl hydroxylase (EC 1.14.11.2). The structure-activity relationships seen with [2,2'-bipyridine]-5-carboxylic acid (4) closely resemble those of pyridine-2-carboxylic acid (2). Accordingly, [2,2'-bipyridine]-5,5'-dicarboxylic acid (11, IC50 = 0.19 microM) is the most potent inhibitor of its type yet reported. However, 2,2'-bipyridines lacking a 5-carboxylate are poor inhibitors. These contrasting structure-activity relationships are discussed in terms of net anionic charge, iron chelation, and the availability of alternative putative binding modes at a single binding site in each catalytic subunit.
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“Whereas bipy itself does not serve as an activator of CP4H,20,22”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [22]
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Cited by
Collagen Prolyl 4-Hydroxylase as a Therapeutic Target: Miniperspective
Vasta, J. D., & Raines, R. T. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00822 · Cited by 82
Selective Inhibition of Collagen Prolyl 4-Hydroxylase in Human Cells
Vasta, J. D., Andersen, K. A., Deck, K. M., Nizzi, C. P., Eisenstein, R. S., & Raines, R. T. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00749 · Cited by 41
Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center
Vasta, J. D., & Raines, R. T. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00251 · Cited by 36
Selective inhibition of prolyl 4-hydroxylases by bipyridinedicarboxylates
Vasta, J. D., & Raines, R. T. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.05.003 · Cited by 16
Metadata
- Authors
- Hales, N. J., & Beattie, J. F.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1993-11
- Volume
- 36
- Issue
- 24
- Pages
- 3853-3858
- ISSN
- 0022-2623
- 1520-4804
- Cited by
- 31
- References
- 0
- Language
- en
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