Frontispiece: Replacement of Water Molecules in a Phosphate Binding Site by Furanoside-Appended lin-Benzoguanine Ligands of tRNA-Guanine Transglycosylase (TGT)
Molecular Recognition In their Full Paper on page 126 ff., G. Klebe, F. Diederich et al. describe a novel series of lin‐benzoguanines that target the polar ribose‐34 pocket of Z. mobilis TGT with a furanosyl moiety. The preparation involved a new cyclization strategy for the lin‐benzoguanine core an...
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Veröffentlicht in: | Chemistry : a European journal 2015-01, Vol.21 (1), p.n/a |
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Hauptverfasser: | , , , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Molecular Recognition In their Full Paper on page 126 ff., G. Klebe, F. Diederich et al. describe a novel series of lin‐benzoguanines that target the polar ribose‐34 pocket of Z. mobilis TGT with a furanosyl moiety. The preparation involved a new cyclization strategy for the lin‐benzoguanine core and the highly challenging separation of the anomeric mixtures by HPLC on a chiral stationary phase. They were designed to replace a conserved water cluster and differ by the functional groups at C(2) and C(3) of the furanosyl moiety being either OH or OMe. |
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ISSN: | 0947-6539 1521-3765 |
DOI: | 10.1002/chem.201580162 |