2. Academic Validation
  3. Molecular characterization of macbecin as an Hsp90 inhibitor

Molecular characterization of macbecin as an Hsp90 inhibitor

  • J Med Chem. 2008 May 8;51(9):2853-7. doi: 10.1021/jm701558c.
Christine J Martin 1,  Sabine Gaisser,  Iain R Challis,  Isabelle Carletti,  Barrie Wilkinson,  Matthew Gregory,  Chrisostomos Prodromou,  S Mark Roe,  Laurence H Pearl,  Susan M Boyd,  Ming-Qiang Zhang
Affiliations

Affiliation

  • 1 Biotica Technology Limited, Chesterford Research Park, Essex CB10 1XL, U.K. [email protected]
PMID: 18357975 DOI: 10.1021/jm701558c
Abstract

Macbecin compares favorably to geldanamycin as an HSP90 Inhibitor, being more soluble, stable, more potently inhibiting ATPase activity (IC50 = 2 microM) and binding with higher affinity (Kd = 0.24 microM). 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 T/C: 32%) in a DU145 murine xenograft. Macbecin thus represents an attractive lead for further optimization.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-107578
    HSP Inhibitor
    HSP