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Antagonistic properties of the suramin analogue NF023 at heterologously expressed P2X receptors
Profiling at recombinant homomeric and heteromeric rat P2X receptors identifies the suramin analogue NF449 as a highly potent P2X1 receptor antagonist
Suramin analogues as subtype-selective G protein inhibitors.
The results show that it is possible to design G protein inhibitors that target the effector binding site on the alpha subunits, and selected suramin is selective for recombinant Gsalpha-s and recombinant Go alpha.
NF449: a subnanomolar potency antagonist at recombinant rat P2X1 receptors
- K. Braun, J. Rettinger, G. Lambrecht
- Biology, ChemistryNaunyn-Schmiedeberg's Archives of Pharmacology
- 1 September 2001
The subnanomolar potency at rP2X1 receptors and the rank order of potency, P 2X1 >> P2X3 > P 2Y1 > P2Y2 > ecto-nucleotidases, make NF449 unique among the P2 receptor antagonists reported to date.
NF449, a novel picomolar potency antagonist at human P2X1 receptors.
The suramin analogue NF279 is a novel and potent antagonist selective for the P2X1 receptor
Gsalpha-selective G protein antagonists.
- M. Hohenegger, M. Waldhoer, M. Freissmuth
- BiologyProceedings of the National Academy of Sciences…
- 6 January 1998
Two compounds, NF503 and NF449, fulfill essential criteria for Gsalpha-selective antagonists and demonstrate the feasibility of subtype- selective G protein inhibition.
Structure-activity relationships of suramin and pyridoxal-5'-phosphate derivatives as P2 receptor antagonists.
This work moves closer to the ideal goal of classifying the recombinant and native P2 receptor subtypes on the basis of antagonist profiles, and focuses on structure-activity relationships of PPADS and suramin analogues.
Suramin and suramin analogs activate skeletal muscle ryanodine receptor via a calmodulin binding site.
It is concluded that NF307 and suramin interact directly with a calmodulin binding domain of the ryanodine receptor, a potent calcium-sensitizing effect that may represent a lead compound in the search of synthetic ryanode receptor ligands.