| Title : The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors - Nordhoff_2006_Bioorg.Med.Chem.Lett_16_1744 |
| Author(s) : Nordhoff S , Cerezo-Galvez S , Feurer A , Hill O , Matassa VG , Metz G , Rummey C , Thiemann M , Edwards PJ |
| Ref : Bioorganic & Medicinal Chemistry Lett , 16 :1744 , 2006 |
|
Abstract :
The co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered. |
| PubMedSearch : Nordhoff_2006_Bioorg.Med.Chem.Lett_16_1744 |
| PubMedID: 16376544 |
| Gene_locus related to this paper: pig-dpp4 |
| Inhibitor | FPB 1-Phenylcyclopentanemethylamine Tetrahydroisoquinoline-derivative |
| Gene_locus | pig-dpp4 |
| Structure | 2BUA 2BUB 2BUC |
Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ (2006)
The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors
Bioorganic & Medicinal Chemistry Lett
16 :1744
Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ (2006)
Bioorganic & Medicinal Chemistry Lett
16 :1744