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

DOI: 10.1016/j.bmcl.2009.01.094

Source and publish data:

Bioorganic and Medicinal Chemistry Letters p. 1694 - 1697 (2009)

Update date:2022-08-04

Topics:

Authors:

Emmitte, Kyle A.

Adjebang, George M.

Andrews, C. Webb

Alberti, Jennifer G. Badiang

Bambal, Ramesh

Chamberlain, Stanley D.

Davis-Ward, Ronda G.

Dickson, Hamilton D.

Hassler, Daniel F.

Hornberger, Keith R.

Jackson, Jeffrey R.

Kuntz, Kevin W.

Lansing, Timothy J.

Mook Jr., Robert A.

Nailor, Kristen E.

Pobanz, Mark A.

Smith, Stephon C.

Sung, Chiu-Mei

Cheung, Mui

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Article abstract of DOI:10.1016/j.bmcl.2009.01.094

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.

Full text of DOI:10.1016/j.bmcl.2009.01.094

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