| Literature DB >> 26117647 |
Michael L Berger1, Dorota Maciejewska2, Jean Jacques Vanden Eynde3, Madhusoodanan Mottamal4, Jerzy Żabiński2, Paweł Kaźmierczak2, Mateusz Rezler2, Ivana Jarak5, Ivo Piantanida5, Grace Karminski-Zamola5, Annie Mayence4, Patrick Rebernik6, Arvind Kumar7, Mohamed A Ismail7, David W Boykin7, Tien L Huang4.
Abstract
The anti-protozoal drug pentamidine is active against opportunistic Pneumocystis pneumonia, but in addition has several other biological targets, including the NMDA receptor (NR). Here we describe the inhibitory potencies of 76 pentamidine analogs at 2 binding sites of the NR, the channel binding site labeled with [(3)H]MK-801 and the [(3)H]ifenprodil binding site. Most analogs acted weaker at the ifenprodil than at the channel site. The spermine-sensitivity of NR inhibition by the majority of the compounds was reminiscent of other long-chain dicationic NR blockers. The potency of the parent compound as NR blocker was increased by modifying the heteroatoms in the bridge connecting the 2 benzamidine moieties and also by integrating the bridge into a seven-membered ring. Docking of the 45 most spermine-sensitive bisbenzamidines to a recently described acidic interface between the N-terminal domains of GluN1 and GluN2B mediating polyamine stimulation of the NR revealed the domain contributed by GluN1 as the most relevant target.Entities:
Keywords: Alkylation; Bisbenzamidine; Coupling; Ifenprodil; Molecular docking; NMDA receptor; Pentamidine; Polyamine; Radioligand binding; Rat brain
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Year: 2015 PMID: 26117647 PMCID: PMC4910395 DOI: 10.1016/j.bmc.2015.06.012
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641