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M.T. Iorio:
"Towards functional selectivity for GABAA receptor subtypes";
Vortrag: 7th Paul Ehrlich MedChem EuroPhD Network Symposium, Vienna; 25.08.2017 - 27.08.2017; in: "7th Paul Ehrlich MedChem EuroPhD Network Symposium", (2017), S. 24.

Gamma- aminobutyric acid type A receptors (GABAA) are pentameric
channel proteins with a high subunit diversity. In mammalian species 19
subunits were identified: six α, three β, three γ, one δ, one ε, one θ, one π and
three ρ. The different subunits can be arranged in various ways to form a
pentamer, and the most accepted combination is assumed to consist of two α,
two β and one γ subunits. [1]
GABAA receptors are targets of many clinically relevant drugs such as benzodiazepine
(BZ), barbiturates and steroids for the treatment of anxiety, depression and epilepsy.
While the benzodiazepines act as positive allosteric modulators via a binding site located at the
α+/γ- interface, its natural agonist -GABA- binds at the β+/α- interfaces (Fig.1) [2]
The pyrazoloquinolinones (Fig.2) bind with high affinity at the BZ binding site,
where they usually act as null modulators and in addition they bind with low
affinity to newly described binding site at the α+/β- interfaces where they act as
positive allosteric modulators (Fig.1).[3]
Here a set of Pyrazoquinolinones with a putative functional selectivity for α6
containing receptors is reported. A series of these compounds with different
substituents in R7 position was synthesized and their behaviour in α6β3γ2
receptors was investigated.

http://publik.tuwien.ac.at/files/publik_264672.pdf