622347-49-3Relevant academic research and scientific papers
Design, synthesis, and structure - Activity relationships for chimeric inhibitors of Hsp90
Shen, Gang,Wang, Mingwen,Welch, Timothy R.,Blagg, Brian S. J.
, p. 7618 - 7631 (2007/10/03)
(Chemical Equation Presented) Inhibition of the 90 kDa heat shock protein (Hsp90) family of molecular chaperones represents a promising new chemotherapeutic approach toward the treatment of several cancers. Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site. The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed. A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.
Selective Synthesis of the para-Quinone Region of Geldanamycin
Andrus, Merritt B.,Hicken, Erik J.,Meredith, Erik L.,Simmons, Bryon L.,Cannon, John F.
, p. 3859 - 3862 (2007/10/03)
(Matrix presented) The quinone portion of the ansamycin geldanamycin was made with complete selectivity from the 1,4-dihydroquinone generated from a 1,4-bis-methoxymethyl (MOM) ether intermediate. Palladium catalysis with air gave the desired product in 9
