An alternative route: The fungal metabolite FR235222, a potent inhibitor of mammalian histone deacetylase (HDAC), has been synthesized. Key steps are the preparation of unusual amino acids Ahoda and (2R,4S)-MePro. A 3D model for cyclopeptide inhibitor interaction with the HDAC active site (see picture) highlights the differences between the binding mode of small-molecule and cyclopeptide inhibitors. (Figure Presented). © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
Total synthesis, NMR solution structure, and binding model of the potent histone deacetylase inhibitor FR235222 / Rodriquez, M.; Terracciano, S.; Cini, E.; Settembrini, G.; Bruno, I.; Bifulco, G.; Taddei, M.; Gomez-Paloma, L.. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - 45:3(2006), pp. 423-427. [10.1002/anie.200501995]
Total synthesis, NMR solution structure, and binding model of the potent histone deacetylase inhibitor FR235222
Rodriquez M.Primo
;
2006
Abstract
An alternative route: The fungal metabolite FR235222, a potent inhibitor of mammalian histone deacetylase (HDAC), has been synthesized. Key steps are the preparation of unusual amino acids Ahoda and (2R,4S)-MePro. A 3D model for cyclopeptide inhibitor interaction with the HDAC active site (see picture) highlights the differences between the binding mode of small-molecule and cyclopeptide inhibitors. (Figure Presented). © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
