title: Affinity-driven selection of tripeptide inhibitors of ribonucleotide reductase.
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.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
authors.forename: Ying
authors.initials: Y
authors.lastname: Gao
authors.forename: Sebastian
authors.initials: S
authors.lastname: Liehr
authors.forename: Barry S
authors.initials: BS
authors.lastname: Cooperman
mesh_terms: 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
chemical_list: D000596:Amino Acids; D004791:Enzyme Inhibitors; D005449:Fluorenes; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D009842:Oligopeptides; D019151:Peptide Library; D021122:Protein Subunits; D012264:Ribonucleotide Reductases