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Recognition of nucleosides at adenosine receptors (ARs) is supported by multiple X-ray structures, but the structure of an adenine complex is unknown. We examined the selectivity of predicted A 1 AR and A 3 AR adenine antagonists that incorporated known agonist affinity-enhancing N  6 and C2 substituents. Adenines with A 1 AR-favoring N  6 -alkyl, cycloalkyl and arylalkyl substitutions combined with an A 3 AR-favoring 2-((5-chlorothiophen-2-yl)ethynyl) group were human (h) A 3 AR-selective, e.g. MRS7497 17 (∼1000-fold over A 1 AR). In addition, binding selectivity over hA 2A AR and hA 2B AR and functional A 3 AR antagonism were demonstrated. 17 was subjected to computational docking and molecular dynamics simulation in a hA 3 AR homology model to predict interactions. The SAR of nucleoside AR agonists was not recapitulated in adenine AR antagonists, and modeling suggested an alternative, inverted binding mode with the key N250 6.55 H-bonding to the adenine N  3 and N  9 , instead of N  6 and N  7 as in adenosine agonists.

Structure activity relationship of 2-arylalkynyl-adenine derivatives as human A3 adenosine receptor antagonists

Structure activity relationship of 2-arylalkynyl-adenine derivatives as human A₃ adenosine receptor antagonists