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001-es BibID:BIBFORM008742
Első szerző:Chrysina, Evangelia D.
Cím:Amide-1,2,3-triazole bioisosterism: the glycogen phosphorylase case / Evangelia D. Chrysina, Éva Bokor, Kyra-Melinda Alexacou, Maria-Despoina Charavgi, George N. Oikonomakos, Spyros E. Zographos, Demetres D. Leonidas, Nikos G. Oikonomakos, László Somsák
Dátum:2009
Megjegyzések:Per-O-acetylated beta-D-glucopyranosyl azide was transformed into an intermediate iminophosphorane by PMe3 which was then acylated to N-acyl-beta-D-glucopyranosylamines. The same azide and substituted acetylenes gave 1-(beta-D-glucopyranosyl)-4-substituted-1,2,3-triazoles in Cu(I)-catalyzed azide-alkyne cycloadditions. Deprotection of these products by the Zemplén method furnished beta-D-Glcp-NHCO-R derivatives as well as 1-(beta-D-Glcp)-4-R-1,2,3-triazoles which were evaluated as inhibitors of rabbit muscle glycogen phosphorylase b. Pairs of amides versus triazoles with the same R group displayed similar inhibition constants. X-ray crystallographic studies on the enzyme-inhibitor complexes revealed high similarities in the binding of pairs with R = 2-naphthyl and hydroxymethyl, while for the R = Ph and 1-naphthyl compounds a different orientation of the aromatic part and changes in the conformation of the 280s loop were observed. By this study new examples of amide-1,2,3-triazole bioisosteric relationship have been provided.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Tetrahedron: Asymmetry. - 20 : 6-8 (2009), p. 733-740. -
További szerzők:Bokor Éva (1982-) (vegyész) Alexacou, Kyra-Melinda Charavgi, Maria-Despoina Oikonomakos, George N. Zographos, Spyros E. Leonidas, Demetres D. Oikonomakos, Nikos G. Somsák László (1954-) (vegyész)
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001-es BibID:BIBFORM006384
Első szerző:Somsák László (vegyész)
Cím:New inhibitors of glycogen phosphorylase as potential antidiabetic agents / L. Somsák, K. Czifrák, M. Tóth, É. Bokor, E. D. Chrysina, K.-M. Alexacou, J. M. Hayes, C. Tiraidis, E. Lazoura, D. D. Leonidas, S. E. Zographos, N. G. Oikonomakos
Dátum:2008
ISSN:0929-8673
Megjegyzések:The protein glycogen phosphorylase has been linked to type 2 diabetes, indicating the importance of this target to human health. Hence, the search for potent and selective inhibitors of this enzyme, which may lead to antihyperglycaemic drugs, has received particular attention. Glycogen phosphorylase is a typical allosteric protein with five different ligand binding sites, thus offering multiple opportunities for modulation of enzyme activity. The present survey is focused on recent new molecules, potential inhibitors of the enzyme. The biological activity can be modified by these molecules through direct binding, allosteric effects or other structural changes. Progress in our understanding of the mechanism of action of these inhibitors has been made by the determination of high-resolution enzyme inhibitor structures (both muscle and liver). The knowledge of the three-dimensional structures of protein-ligand complexes allows analysis of how the ligands interact with the target and has the potential to facilitate structure-based drug design. In this review, the synthesis, structure determination and computational studies of the most recent inhibitors of glycogen phosphorylase at the different binding sites are presented and analyzed.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
glycogen phosphorylase
inhibitor
type 2 diabetes
structure-based drug design
antidiabetic agent
Megjelenés:Current Medicinal Chemistry. - 15 : 28 (2008), p. 2933-2983. -
További szerzők:Czifrák Katalin (1978-) (vegyész) Tóth Marietta (1974-) (vegyész) Bokor Éva (1982-) (vegyész) Chrysina, Evangelia D. Alexacou, Kyra-Melinda Hayes, Joseph M. Tiraidis, Costantinos Lazoura, E. Leonidas, Demetres D. Zographos, Spyros E. Oikonomakos, George N.
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