A series of N-linked tetrakis(tetrapeptido)calix[4]arene diversomers, 3A–P, has been synthesized by coupling of a cone calix[4]arene tetracarboxylic acid chloride with tetrapeptides 1A–P obtained in a parallel fashion. The inhibition activity of 3A–P towards tissue and microbial transglutaminase was evaluated by in vitro assays with a labeled substrate. Kinetic analysis using one of the most active derivatives (3A) showed a noncompetitive inhibition with respect to the amino acceptor substrate and an uncompetitive inhibition with respect to amino donor substrate. Experimental results are in accordance with an inhibition due to a protein specific surface recognition on a region noncomprising the enzyme active site.

Transglutaminase surface recognition by peptidocalix[4]arene diversomers

CAPUTO, Ivana;ESPOSITO, Carla;MARTINO, Marco;GAETA, CARMINE;TROISI, FRANCESCO;NERI, Placido
2005

Abstract

A series of N-linked tetrakis(tetrapeptido)calix[4]arene diversomers, 3A–P, has been synthesized by coupling of a cone calix[4]arene tetracarboxylic acid chloride with tetrapeptides 1A–P obtained in a parallel fashion. The inhibition activity of 3A–P towards tissue and microbial transglutaminase was evaluated by in vitro assays with a labeled substrate. Kinetic analysis using one of the most active derivatives (3A) showed a noncompetitive inhibition with respect to the amino acceptor substrate and an uncompetitive inhibition with respect to amino donor substrate. Experimental results are in accordance with an inhibition due to a protein specific surface recognition on a region noncomprising the enzyme active site.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11386/1058698
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