Affinity-driven selection of tripeptide inhibitors of ribonucleotide reductase.
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.
Gao
Ying
Y
Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Liehr
Sebastian
S
Cooperman
Barry S
BS
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D004791:Enzyme Inhibitors / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D005449:Fluorenes / Q000737:chemistry; D051379:Mice; D009842:Oligopeptides / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D019151:Peptide Library; D021122:Protein Subunits; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D004791:Enzyme Inhibitors; D005449:Fluorenes; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D009842:Oligopeptides; D019151:Peptide Library; D021122:Protein Subunits; D012264:Ribonucleotide Reductases