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Piperazine modification in 2,4,6-triaminopyrimidine derivatives as histamine H4 receptor ligands.

The human histamine H4 receptor (hH4R) is a promising new target in the therapy of inflammatory and immunomodulatory diseases. The 2,4,6-triaminopyrimidine structure has been established as a potent hH4R affinity scaffold. By using the inverse agonist ST-1012 as reference ligand, piperazine modifications were performed to get larger structural variations. Therefore, different spacers were introduced into the lead structure and the influence on affinity of this basic element was evaluated. While a short distance between aminopyrimidine and basic moiety is beneficial, a lipophilic group in the eastern part is necessary to maintain hH4R affinity.