New work by scientists from Florida State University, Tallahassee and the University of London's Birkbeck College provides further insight into the mechanism of action of the anticancer drug Taxol and could facilitate the design of new drugs (J. Mol. Biol. 285: 197–203, 1999). The cytoskeletal protein tubulin has long been known as a cellular target for Taxol, but it has been unclear how this interaction results in the death of cancer cells. Lee Makowski and his colleagues set out to identify other cellular targets of Taxol to gain better insight into how it works. The team screened a 12 amino acid phage–displayed peptide library of cellular proteins and identified over 70 peptide clones with affinity to Taxol. After sequencing the clones and searching for similarities to human protein sequences, they found that one–third had significant similarity to the disordered loop region of the BCL–2 protein, which is involved in apoptosis. ELISA–binding assays showed that the selected peptides were predictive of Taxol–binding sites in BCL–2. First author, Diane Rodi says "We are excited about this simple in vitro screen because it has the potential for identifying all molecular targets of a drug before it is tested in animals or humans." The group is characterizing additional clones identified in the screen and plans to investigate further how the drug's interaction with BCL–2 is involved in killing cancer cells.