Designed calix[8]arene-based ligands for selective tryptase surface recognition.
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.
Mecca
Tommaso
T
Istituto di Chimica Biomolecolare (sez. di Catania), CNR, Via del Santuario 110, I-95028 Valverde (CT), Italy.
Consoli
Grazia M L
GM
Geraci
Corrada
C
Cunsolo
Francesca
F
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
D008024:Ligands; D015842:Serine Proteinase Inhibitors; D047250:Calixarenes; D012697:Serine Endopeptidases; D053802:Tryptases