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Updated: Aug 19, 2026

Determining the Serum Stability of Human Adenosine Deaminase 1 Enzyme
Published on: September 27, 2024
Exploring human adenosine A3 receptor complementarity and activity for adenosine analogues modified in the ribose and
Philippe Van Rompaey1, Kenneth A Jacobson, Ariel S Gross
1Laboratory for Medicinal Chemistry, Faculty of Pharmaceutical Sciences (FFW), Ghent University, Harelbekestraat 72, B-9000 Gent, Belgium.
Abstract:
In this paper we investigated the influence on affinity, selectivity and intrinsic activity upon modification of the adenosine agonist scaffold at the 3'- and 5'-positions of the ribofuranosyl moiety and the 2- and N6-positions of the purine base. This resulted in the synthesis of various analogues, that is, 3-12 and 24-33, with good hA3AR selectivity and moderate-to-high affinities (as in 32, Ki=27 nM). Interesting was the ability to tune the intrinsic activity depending on the substituent introduced at the 3'-position.
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