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PubMed · 15351389

Designed calix[8]arene-based ligands for selective tryptase surface recognition.

Tommaso Mecca·Grazia M L Consoli·Corrada Geraci·Francesca Cunsolo
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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.

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Binding, CompetitiveCalixarenesComputer SimulationDrug DesignHumansKineticsLigandsLungModels, MolecularSerine EndopeptidasesSerine Proteinase InhibitorsTryptasesJournal Article

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Tommaso Mecca, Grazia M L Consoli, Corrada Geraci, Francesca Cunsolo. 2004-10-01. Designed calix[8]arene-based ligands for selective tryptase surface recognition.. https://doi.org/10.1016/j.bmc.2004.07.037

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