2. Academic Validation
  3. Non-charged thiamine analogs as inhibitors of enzyme transketolase

Non-charged thiamine analogs as inhibitors of enzyme transketolase

  • Bioorg Med Chem Lett. 2008 Jan 15;18(2):509-12. doi: 10.1016/j.bmcl.2007.11.098.
Allen A Thomas 1,  J De Meese,  Y Le Huerou,  Steven A Boyd,  Todd T Romoff,  Steven S Gonzales,  Indrani Gunawardana,  Tomas Kaplan,  Francis Sullivan,  Kevin Condroski,  Joseph P Lyssikatos,  Thomas D Aicher,  Josh Ballard,  Bryan Bernat,  Walter DeWolf,  May Han,  Christine Lemieux,  Darin Smith,  Solly Weiler,  S Kirk Wright,  Guy Vigers,  Barb Brandhuber
Affiliations

Affiliation

  • 1 Array BioPharma Inc., 3200 Walnut Street, Boulder, CO 80301, USA. athomas@arraybiopharma.com
PMID: 18182286 DOI: 10.1016/j.bmcl.2007.11.098
Abstract

Inhibition of the thiamine-utilizing enzyme Transketolase (TK) has been linked with diminished tumor cell proliferation. Most thiamine antagonists have a permanent positive charge on the B-ring, and it has been suggested that this charge is required for diphosphorylation by thiamine pyrophosphokinase (TPPK) and binding to TK. We sought to make neutral thiazolium replacements that would be substrates for TPPK, while not necessarily needing thiamine transporters (ThTr1 and ThTr2) for cell penetration. The synthesis, SAR, and structure-based rationale for highly potent non-thiazolium TK antagonists are presented.

Figures
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  • HY-16339
    99.56%, 转酮醇酶抑制剂
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