Design of potent thiophene inhibitors of polo-like kinase 1 with improved solubility and reduced protein binding

  • Bioorg Med Chem Lett. 2009 Mar 15;19(6):1694-7. doi: 10.1016/j.bmcl.2009.01.094.
Kyle A Emmitte  1 ,  George M Adjabeng ,  C Webb Andrews ,  Jennifer G Badiang Alberti ,  Ramesh Bambal ,  Stanley D Chamberlain ,  Ronda G Davis-Ward ,  Hamilton D Dickson ,  Daniel F Hassler ,  Keith R Hornberger ,  Jeffrey R Jackson ,  Kevin W Kuntz ,  Timothy J Lansing ,  Robert A Mook Jr ,  Kristen E Nailor ,  Mark A Pobanz ,  Stephon C Smith ,  Chiu-Mei Sung ,  Mui Cheung
Affiliations
  • 1. Five Moore Drive, Research Triangle Park, NC 27709, GlaxoSmithKline, USA.
PMID: 19237286 DOI: 10.1016/j.bmcl.2009.01.094
Abstract

A series of thiophene PLK1 inhibitors was optimized for increased solubility and reduced protein binding through the appendage of basic amine functionality. Interesting selectivity between PLK1 and PLK3 was also obtained through these modifications.

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