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Affinity-driven selection of tripeptide inhibitors of ribonucleotide reductase
Ying Gao1, Sebastian Liehr, Barry S Cooperman
1Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Bioorganic & Medicinal Chemistry Letters
|February 15, 2002
Abstract:
Tripeptide libraries of the type Fmoc(W/F)XF were screened for binding to the large subunit of mouse ribonucleotide reductase (mRR), using a new, affinity chromatography method. A high-affinity tripeptide, FmocWFF, was found that inhibited mRR activity with a K(i) equal to that of AcFTLDADF, the heptapeptide corresponding to the C-terminus of the small subunit of mRR.