rp8brpetcgmps

cGMP-dependent protein kinase (PKG) inhibitor

Rp-8-CPT-cAMP is a structural combination of the lipophilic and non-hydrolyzable cAMP analogs, 8-CPT-cyclic AMP and Rp-cyclic AMPS .[1] It functions as a site-selective inhibitor of protein kinase A (PKA) type I and II, with preference towards site A of type I and site B of type II.2 By occupying cAMP binding sites at the regulatory subunit of PKA, Rp-8-CPT-cAMP prevents the kinase holoenzyme from dissociative activation.[2],[3]

Rp-8-bromo-Cyclic AMPS (Rp-8-bromo-cAMPS) is a cell-permeable cAMP analog that combines an exocyclic sulfur substitution in the equatorial position of the cyclophosphate ring with a bromine substitution in the adenine base of cAMP. It acts as an antagonist of cAMP-dependent protein kinases (PKAs) and is resistant to hydrolysis by cyclic nucleotide phosphodiesterases. Rp-8-bromo-cAMPS more effectively antagonizes cAMP-dependent activation of purified PKA type I from rabbit muscle than PKA type II from bovine heart.

Rp-8-Br-cAMPS acts as an inhibitor of PKA. By binding to the cAMP binding sites on the regulatory subunits, Rp-8-Br-cAMPS prevents the dissociation and activation of PKA. Additionally, it enhances immune function in mouse models of retroviral infection.

Rp-8-pCPT-cGMPS is a competitive inhibitor of cyclic guanosine monophosphate (cGMP)-dependent protein kinase (PKG) with a Ki of 0.5 μM. This compound exhibits increased lipophilicity, allowing it to penetrate cell membranes more readily and achieve sufficient intracellular concentrations to inhibit PKG. Rp-8-pCPT-cGMPS is useful for researching the activity and function of PKG in platelets.

Rp-8-Br-cGMPS (Rp-8-bromo-Cyclic GMPS) sodium salt acts as an effective activator of Ca2+-ATPase. Additionally, it serves as an agonist for rod CNG channels and an inhibitor of PKG. Rp-8-Br-cGMPS sodium salt mediates the reduction of cytoplasmic Ca2+ by activating the Ca2+-ATPase enzyme, consequently removing Ca2+ from the cell.

Rp-8-CPT-cAMPS is a powerful and competitive antagonist of cAMP-induced activation of cAMP-dependent protein kinase (PKA) I and II. Acting as a potent cAMP analog, Rp-8-CPT-cAMPS exhibits a preference for site A of RI over site A of RII. Additionally, it favors site B of RII over site B of RI. This compound effectively inhibits cAMP-dependent PKA activation and demonstrates selectivity in binding to specific sites within the protein kinase.