title: Designed calix[8]arene-based ligands for selective tryptase surface recognition.
abstract: Basic amino acid calix[8]arene receptors for tryptase surface recognition have been synthesized. The tetrameric arrangement and the negative charge distribution close to the active sites of the enzyme, have suggested the design of complementary multifunctional receptors that might bind to the active region of the protein blocking the approach of the substrate. Kinetic inhibition analysis on recombinant lung tryptase have showed a time-dependent competitive inhibition with both initial and steady-state rate constants in the nanomolar range.
authors.affiliation: Istituto di Chimica Biomolecolare (sez. di Catania), CNR, Via del Santuario 110, I-95028 Valverde (CT), Italy.
authors.forename: Tommaso
authors.initials: T
authors.lastname: Mecca
authors.forename: Grazia M L
authors.initials: GM
authors.lastname: Consoli
authors.forename: Corrada
authors.initials: C
authors.lastname: Geraci
authors.forename: Francesca
authors.initials: F
authors.lastname: Cunsolo
mesh_terms: D001667:Binding, Competitive; D047250:Calixarenes / Q000737:chemistry*; D003198:Computer Simulation; D015195:Drug Design; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008168:Lung / Q000201:enzymology; D008958:Models, Molecular; D012697:Serine Endopeptidases / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D053802:Tryptases
chemical_list: D008024:Ligands; D015842:Serine Proteinase Inhibitors; D047250:Calixarenes; D012697:Serine Endopeptidases; D053802:Tryptases