Molecular characterization of macbecin as an Hsp90 inhibitor

Martin, Christine J, Gaisser, Sabine, Challis, Iain R, Carletti, Isabelle, Wilkinson, Barrie, Gregory, Matthew, Prodromou, Chrisostomos, Roe, S Mark, Pearl, Laurence H, Boyd, Susan M and Zhang, Ming-Qiang (2008) Molecular characterization of macbecin as an Hsp90 inhibitor. Journal of Medicinal Chemistry, 51 (9). pp. 2853-2857. ISSN 0022-2623

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Macbecin compares favorably to geldanamycin as an Hsp90 inhibitor, being more soluble, stable, more potently inhibiting ATPase activity (IC50 = 2 mu M) and binding with higher affinity (K-d = 0.24 mu M). Structural studies reveal significant differences in their Hsp90 binding characteristics, and macbecin-induced tumor cell growth inhibition is accompanied by characteristic degradation of Hsp90 client proteins. Macbecin significantly reduced tumor growth rates (minimum TIC: 32%) in a DU145 murine xenograft. Macbecin thus represents an attractive lead for further optimization.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Depositing User: Chrisostomos Prodromou
Date Deposited: 06 Feb 2012 20:36
Last Modified: 29 Oct 2012 09:48
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