Tailored fragments of roseophilin selectively antagonize Mcl-1 in vitro .

Autor: Bracken JD; Department of Chemistry and Biochemistry, University of California at Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, United States., Carlson AD; Department of Chemistry and Biochemistry, University of California at Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, United States., Frederich JH; Department of Chemistry and Biochemistry, University of California at Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, United States., Nguyen M; Department of Biochemistry and Goodman Cancer Research Center, McGill University, Montréal, Québec, Canada., Shore GC; Department of Biochemistry and Goodman Cancer Research Center, McGill University, Montréal, Québec, Canada., Harran PG; Department of Chemistry and Biochemistry, University of California at Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, United States.
Jazyk: angličtina
Zdroj: Tetrahedron letters [Tetrahedron Lett] 2015 Jun 03; Vol. 56 (23), pp. 3612-3616.
DOI: 10.1016/j.tetlet.2015.01.191
Abstrakt: We have discovered a fragment of the natural product roseophilin, a member of the prodiginine family, that antagonizes Mcl-1 functions in a liposome-based assay for mitochondrial membrane permeabilization. By tailoring this substance such that it can participate in salt bridging with the protein surface, we have prepared the first prodiginine inspired structure that shows direct, saturable binding to a recombinant Bcl-2 family member in vitro .
Databáze: MEDLINE
Externí odkaz: