Design of noncompetitive interleukin-8 inhibitors acting on CXCR1 and CXCR2

  • J Med Chem. 2007 Aug 23;50(17):3984-4002. doi: 10.1021/jm061469t.
Alessio Moriconi  1 ,  Maria Candida Cesta ,  Maria Neve Cervellera ,  Andrea Aramini ,  Silvia Coniglio ,  Sandro Colagioia ,  Andrea Rosario Beccari ,  Cinzia Bizzarri ,  Michela Rita Cavicchia ,  Massimo Locati ,  Emanuela Galliera ,  Paola Di Benedetto ,  Paolo Vigilante ,  Riccardo Bertini ,  Marcello Allegretti
Affiliations
  • 1. Research Centre, Dompé pha.r.ma s.p.a., via Campo di Pile, 67100, L'Aquila, Italy.
Abstract

Chemokines CXCL8 and CXCL1 play a key role in the recruitment of neutrophils at the site of inflammation. CXCL8 binds two membrane receptors, CXCR1 and CXCR2, whereas CXCL1 is a selective agonist for CXCR2. In the past decade, the physiopathological role of CXCL8 and CXCL1 has been investigated. A novel class of small molecular weight allosteric CXCR1 inhibitors was identified, and reparixin, the first drug candidate, is currently under clinical investigation in the prevention of ischemia/reperfusion injury in organ transplantation. Reparixin binding mode to CXCR1 has been studied and used for a computer-assisted design program of dual allosteric CXCR1 and CXCR2 inhibitors. In this paper, the results of modeling-driven SAR studies for the identification of potent dual inhibitors are discussed, and three new compounds (56, 67, and 79) sharing a common triflate moiety have been selected as potential leads with optimized pharmacokinetic characteristics.

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