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Solid phase synthesis of anthraquinone peptides and their evaluation as topoisomerase I inhibitors
Author(s) -
Giles Gregory I.,
Sharma Ram P.
Publication year - 2005
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.635
Subject(s) - moiety , topoisomerase , anthraquinone , combinatorial chemistry , chemistry , peptide , solid phase synthesis , enzyme , peptide synthesis , biochemistry , stereochemistry , organic chemistry
Anthraquinone peptide derivatives have previously been shown to inhibit the enzyme topoisomerase I (topo I), a pharmaceutical target for the prevention of malignant carcinomas. A highly efficient procedure for the attachment of the anthraquinone moiety to the N ‐terminus of a peptide on a solid support is reported. This methodology provides a convenient method for the synthesis of labelled peptides, with potential applications for chemotherapy, DNA detection and protein purification. As the synthetic strategy utilizes the solid phase, it should also be amenable to the generation of combinatorial libraries. The utility of the method by synthesizing a pool of peptides and assaying for topo I inhibition is demonstrated. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.