25840-83-9Relevant articles and documents
Structure-activity relationship of S-trityl-L-cysteine analogues as inhibitors of the human mitotic kinesin Eg5
DeBonis, Salvatore,Skoufias, Dimitrios A.,Indorato, Rose-Laure,Liger, Fran?ois,Marquet, Bernard,Laggner, Christian,Joseph, Beno?t,Kozielski, Frank
, p. 1115 - 1125 (2008/09/20)
The human kinesin Eg5 is a potential drug target for cancer chemotherapy. Eg5 specific inhibitors cause cells to block in mitosis with a characteristic monoastral spindle phenotype. Prolonged metaphase block eventually leads to apoptotic cell death. S-trityl-L-cysteine (STLC) is a tight-binding inhibitor of Eg5 that prevents mitotic progression. It has proven antitumor activity as shown in the NCI 60 tumor cell line screen. It is of considerable interest to define the minimum chemical structure that is essential for Eg5 inhibition and to develop more potent STLC analogues. An initial structure-activity relationship study on a series of STLC analogues reveals the minimal skeleton necessary for Eg5 inhibition as well as indications of how to obtain more potent analogues. The most effective compounds investigated with substitutions at the para-position of one phenyl ring have an estimated Kiapp of 100 nM in vitro and induce mitotic arrest with an EC50 of 200 nM.
Oxazole and thiazole combinatorial libraries
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Page/Page column 10; Sheet 3, (2008/06/13)
This invention provides a novel method for synthesizing an ensemble of peptides that allows for the generation of an unlimited number of antibiotic compounds. More specifically, the method comprises utilizes synthetic heterocyclic amino acids containing thaizole and/or oxazole as building blocks in a solid phase combinatorial synthesis to yield natural and unnatural antibiotic compounds.
