title: Synthesis and biological activity of cyclic peptide inhibitors of ribonucleotide reductase.
abstract: [formula: see text] A series of lactam-bridged peptide inhibitors (2-6) of mammalian ribonucleotide reductase (mRR) has been designed and synthesized on the basis of the heptapeptide N-AcFTLDADF (1), corresponding to the C-terminus of the R2 subunit of mRR. Inhibition studies revealed a direct relation between ring size and activity, with peptide 5 being 2.5 times more potent than peptide 1.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
authors.forename: S
authors.initials: S
authors.lastname: Liehr
authors.forename: J
authors.initials: J
authors.lastname: Barbosa
authors.forename: A B
authors.initials: AB
authors.lastname: Smith
authors.forename: B S
authors.initials: BS
authors.lastname: Cooperman
mesh_terms: D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D006860:Hydrogen Bonding; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
chemical_list: D004791:Enzyme Inhibitors; D010456:Peptides, Cyclic; D012264:Ribonucleotide Reductases